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ATP + H2O
ADP + phosphate
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Q9X0S9; Q9X2F5
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the putative helical domain of the nucleotide binding domains is involved, through its conformational changes, in the coupling between the transmembrane domains and the ATP binding/hydrolysis at the nucleotide-binding domains
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the peripheral membrane protein MalK associates with integral cytoplasmic membrane proteins MalF and MalG to form the maltose transport complex MalFGK. In addition malK participates in two different regulatory pathways which modulate mal gene expression and MalFGK transport activity
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
molecular dynamics simulations to study the ATP-driven association of the NBDs of the maltose ABC transporter, MalK, based on the crystal structures of its open and semiopen dimers, MgATP-dependent opening and closure, mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
extracytoplasmic anchoring of the substrate binding protein, the receptor, is emerging as key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle, molecular mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
maltose transport and ATPase activity of the MalFGK2 complex
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
structure and transport mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the transmembrane protein MalF, MalF-P2, of the maltose ATP-binding cassette transporter MalFGK2-E as an important element in the recognition of substrate by the maltose-binding protein MalE. MalF-P2 is not only responsible for substrate recognition, but also directly involved in activation of substrate transport. Substrate transport model for MalFGK2-E, isothermal titration calorimetry and molecular dynamics simulation, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
translocation of maltose across biological membranes
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
signal-transducing protein EIIAGlc interacts with the MalK subunits of the maltose ATP-binding cassette transporter
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP
-
-
?
additional information
?
-
-
interactions of MalK with the regulatory proteins MalT and enzyme IIAglc
-
-
?
additional information
?
-
-
concomitantly with the three conformations of the ATP-binding cassette MalK2, three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide-binding and periplasmic docking of liganded MalE to MalFG, overview
-
-
?
additional information
?
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
additional information
?
-
quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview
-
-
?
additional information
?
-
-
the periplasmic loop P2 of subunit MalF interacts with the maltose-binding potein MalE independently of the transmembrane region of MalF and MalG in the presence and absence of substrate, overview
-
-
?
additional information
?
-
the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity
-
-
?
additional information
?
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
additional information
?
-
-
although MalF and MalG differ in the number of transmembrane segments of 8 and 6, respectively, and their amino acid sequences, both contain the so-called EAA-motif, i.e. L-loop or coupling helix, which is in contact with MalK. MalF and MalG form a large central cavity for transport, but maltose is only bound to MalF. The MalK subunits bind and hydrolyze ATP, thereby generating the power stroke necessary for the rearrangements of MalFG, quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview
-
-
?
additional information
?
-
-
the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
additional information
?
-
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Q9X0S9; Q9X2F5
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the peripheral membrane protein MalK associates with integral cytoplasmic membrane proteins MalF and MalG to form the maltose transport complex MalFGK. In addition malK participates in two different regulatory pathways which modulate mal gene expression and MalFGK transport activity
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
extracytoplasmic anchoring of the substrate binding protein, the receptor, is emerging as key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle, molecular mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
translocation of maltose across biological membranes
-
-
?
additional information
?
-
-
interactions of MalK with the regulatory proteins MalT and enzyme IIAglc
-
-
?
additional information
?
-
-
concomitantly with the three conformations of the ATP-binding cassette MalK2, three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide-binding and periplasmic docking of liganded MalE to MalFG, overview
-
-
?
additional information
?
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
additional information
?
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
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multimer
-
the maltose transporter consists of a periplasmic maltose binding protein and a multisubunit membrane transporter, MalFGK2
?
x * 42977, calculated from nucleotide sequence
?
1 * 66000 + 1 * 25000 + 2 * 42000, SDS-PAGE
?
-
1 * 66000 + 1 * 25000 + 2 * 42000, SDS-PAGE
-
?
-
F,G,K2, the maltose transport system consists of the periplasmic maltose-binding protein and the membrane proteins MalF, MalG, and MalK which form a heterotetrameric complex in the cytoplasmic membrane
?
-
the binding protein-dependent transport system for maltose and maltodextrins is composed of five proteins: LamB, MalE, MalF, MalG, and MalK
?
-
F,G,K2, the three membrane-associated components of the transport system MalF, MalG and MalK behave as a multiprotein complex
?
-
the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit
dimer
MalK shows three different dimeric conformations
dimer
MalK structure comparison, the enzyme contains two cystathione beta-synthetase domains
additional information
-
MalF subunit structure analysis by NMR
additional information
MalK-derived homology model, overview
additional information
-
MalK-derived homology model, overview
additional information
the enzyme complex consists of two MalKs, MalF, MalG, and MBP, determination and analysis of the in-complex conformation of MalK. Walker A motif, the Q-loop, the LSGGQ motif, and the D-loop display low B-factors, dynamic behavior of the system, detailed overview
additional information
-
the enzyme complex consists of two MalKs, MalF, MalG, and MBP, determination and analysis of the in-complex conformation of MalK. Walker A motif, the Q-loop, the LSGGQ motif, and the D-loop display low B-factors, dynamic behavior of the system, detailed overview
additional information
the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE
additional information
maltose transporter in the inward-facing conformation with rotation axes iand in outward-facing structure, overview
additional information
the maltose/maltodextrin transport system is composed of periplasmic maltose-binding protein, MalE, the pore-forming subunits MalF and MalG, and a homodimer of the nucleotide-binding subunit, MalK, overall structure, component interactions, and comparison, detailed overview. Structure modelling. The MalK dimer provides the energy for maltose transport by hydrolysing ATP. The structure of MalK is solved in two (nucleotide-free) apo-states, one ADP-bound and one ATP-bound state, representing two open, a semi-open and a closed conformation of the dimer, respectively, dynamics, overview
additional information
-
the maltose transporter is an importer composed of two transmembrane subunits, MalF and MalG, and two subunits of a cytoplasmic adenosine triphosphatase (ATPase), MalK
additional information
-
the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE
additional information
-
the maltose/maltodextrin transport system is composed of periplasmic maltose-binding protein, MalE, the pore-forming subunits MalF and MalG, and a homodimer of the nucleotide-binding subunit, MalK, overall structure, component interactions, and comparison, detailed overview. Structure modelling.. The MalK dimer provides the energy for maltose transport by hydrolysing ATP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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C40S/S83C
-
site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E
D380G
-
substitution of aspartate for glycine in the maltose-binding site of MalF likely generates a futile cycle by preventing maltose from binding to MalFGK2 during the catalytic cycle
E159
the E159Q substitution in MalK prevents ATP from being hydrolysed. This results in an ATP-bound structure, which is thought to represent the transition state for ATP hydrolysis. The crystal shows an open (unliganded) MalE bound to the periplasmic side of the complex, a maltose molecule bound solely to a transmembrane region of MalF, and a closed conformation of the ATP-bound MalK(E59Q)2 subunits
E159Q
-
the transporter containing the MalK-E159Q mutation is defective in ATP hydrolysis
E313C
-
leads to a disulfide bond, no effect to ATPase activity
L135F/I154S
-
the binding-protein-independent mutant of Escherichia coli maltose transporter MalFGK2 retains specificity for maltose and shows a high basal ATPase activity in the absence of maltose binding protein
S205C/S252C
-
site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E
T31C/S205C
-
site-directed mutagensis, formation of a crosslink betwwen the mutant subunits
T31C/T177C
-
site-directed mutagenesis, the distance between MalF mutant and MalE T31C mutant changes from 10 A to 5 A upon binding of ATP or maltose, with a less pronounced result, and is reset to 10 A after hydrolysis of one ATP
T80C/S205C
-
site-directed mutagenesis, the mutation of subunit MalF mutant S205C does not affect the interaction with MalE mutant T80C
W230C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
W340C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
W62C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retains good function in maltose transport and MBP-stimulated ATPase activities
Y155C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
Y341C
-
site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retaines good function in maltose transport and MBP-stimulated ATPase activities
D123A
-
the mutant shows wild type activity
E120A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
E120A/D123A/E167A
-
the mutations eliminate uphill maltose transport
E120N/D123N/E167N
-
the mutations eliminate uphill maltose transport
E120Q
-
the mutant shows reduced activity compared to the wild type enzyme
E120Q/D123Q/E167Q
-
the mutations eliminate uphill maltose transport
E167A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
E167Q
-
the mutant shows severely reduced activity compared to the wild type enzyme
D123A
-
the mutant shows wild type activity
-
E120A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
E120Q
-
the mutant shows reduced activity compared to the wild type enzyme
-
E167A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
E167Q
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
T31C/S205C
-
site-directed mutagensis, formation of a crosslink betwwen the mutant subunits
T31C/T177C
-
site-directed mutagenesis, the distance between MalF mutant and MalE T31C mutant changes from 10 A to 5 A upon binding of ATP or maltose, with a less pronounced result, and is reset to 10 A after hydrolysis of one ATP
T80C/S205C
-
site-directed mutagenesis, the mutation of subunit MalF mutant S205C does not affect the interaction with MalE mutant T80C
G137A
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
G137T
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
G137V
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
Q140L
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, fails to hydrolyze ATP and exhibits a strong intrinsic resistance to trypsin in the absence of MgATP, suggesting a drastically altered conformation
Q140N
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140N variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity
Q140K
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140K variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity
Q140K
-
normal intrinsic ATPase activity in soluble state but no hydrolysis of ATP when assembled with MalFG
additional information
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construction of a fusion protein of MalE and the hydrophobic membrane protein MalG
additional information
-
analysis of a collection of MalG insertion mutants
additional information
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insertion mutants: the insertion introduce 31 mostly hydrophilic amino acids into the protein. MalK mutants with insertion after residues 275, 291, 346 and 364, apparently have lost the ability to participate in MalT-dependent mal gene regulation
additional information
-
cystein-free enzyme shows no change in activity compared to wild-type enzyme
additional information
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the MalK2 ATP hydrolysis cycle does not induce MalF-P2 loop rearrangements in the absence of MalE
additional information
-
in deletion mutant MalG-DELTAscoop a four-residue deletion of a periplasmic loop of MalG limits its reach into the maltose-binding pocket of MBP, allowing maltose to remain associated with MBP during the catalytic cycle. Uncoupling of transport and ATP hydrolysis in the MalG-DELTAscoop and MalF-G380D mutants, overview
additional information
-
generation of a series of spontaneous mutants of Lactococcus lactis IL1403 with a large deletion in a chromosomal region involved in carbohydrate metabolism. The mutants show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
additional information
-
generation of a series of spontaneous mutants of Lactococcus lactis IL1403 with a large deletion in a chromosomal region involved in carbohydrate metabolism. The mutants show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
-
additional information
-
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
additional information
-
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
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Escherichia coli
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Escherichia coli
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Escherichia coli
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Escherichia coli
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Maltose and maltodextrin transport in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius is mediated by a high-affinity transport system that includes a maltose binding protein tolerant to low pH
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Alicyclobacillus acidocaldarius
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Reich-Slotky, R.; Panagiotidis, C.; Reyes, M.; Shuman, H.A.
The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
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Escherichia coli
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Escherichia coli
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Escherichia coli
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Functional consequences of mutation in the conserved signature sequence of the ATP-binding-cassette protein MalK
Eur. J. Biochem.
266
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Salmonella enterica subsp. enterica serovar Typhimurium
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Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK2) of Salmonella typhimurium
Biochim. Biophys. Acta
1565
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2002
Salmonella enterica subsp. enterica serovar Typhimurium
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Functional reconstitution of a maltose ATP-binding cassette transporter from the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius
Biochim. Biophys. Acta
1656
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2004
Alicyclobacillus acidocaldarius (Q70HW1), Alicyclobacillus acidocaldarius
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Greller, G.; Riek, R.; Boos, W.
Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis
Eur. J. Biochem.
268
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2001
Thermococcus litoralis
brenda
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Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit
Eur. J. Biochem.
269
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2002
Salmonella enterica subsp. enterica serovar Typhimurium
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Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two malK subunits in the maltose transport complex
J. Biol. Chem.
278
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2003
Escherichia coli
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Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport
J. Biol. Chem.
279
28243-28250
2004
Escherichia coli
brenda
Schoenert, S.; Seitz, S.; Krafft, H.; Feuerbaum, E.; Andernach, I.; Witz, G.; Dahl, M.K.
Maltose and maltodextrin utilization by Bacillus subtilis
J. Bacteriol.
188
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2006
Bacillus subtilis
brenda
Joly, N.; Boehm, A.; Boos, W.; Richet, E.
MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding
J. Biol. Chem.
279
33123-33130
2004
Escherichia coli
brenda
Horn, C.; Jenewein, S.; Tschapek, B.; Bouschen, W.; Metzger, S.; Bremer, E.; Schmitt, L.
Monitoring conformational changes during the catalytic cycle of OpuAA, the ATPase subunit of the ABC transporter OpuA from Bacillus subtilis
Biochem. J.
412
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2008
Escherichia coli (P68187), Escherichia coli
brenda
Blueschke, B.; Volkmer-Engert, R.; Schneider, E.
Topography of the surface of the signal-transducing protein EIIAGlc that interacts with the MalK subunits of the maltose ATP-binding cassette transporter (MalFGK2) of Salmonella typhimurium
J. Biol. Chem.
281
12833-12840
2006
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Oloo, E.O.; Fung, E.Y.; Tieleman, D.P.
The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter
J. Biol. Chem.
281
28397-28407
2006
Escherichia coli
brenda
Jacso, T.; Grote, M.; Daus, M.; Schmieder, P.; Keller, S.; Schneider, E.; Reif, B.
The periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE
Biochemistry
48
2216-2225
2009
Escherichia coli
brenda
Grote, M.; Bordignon, E.; Polyhach, Y.; Jeschke, G.; Steinhoff, H.J.; Schneider, E.
A comparative electron paramagnetic resonance study of the nucleotide-binding domains catalytic cycle in the assembled maltose ATP-binding cassette importer
Biophys. J.
95
2924-2938
2008
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P68187)
brenda
Daus, M.L.; Grote, M.; Schneider, E.
The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle
J. Bacteriol.
191
754-761
2009
Escherichia coli, Salmonella enterica
brenda
Grote, M.; Polyhach, Y.; Jeschke, G.; Steinhoff, H.J.; Schneider, E.; Bordignon, E.
Transmembrane signaling in the maltose ABC transporter MALFGK2-E: The periplasmic MALF-P2 loop communicates substrate availability to the ATP-bound malk dimer
J. Biol. Chem.
284
17521-17526
2009
Escherichia coli
brenda
Lukman, S.; Grant, G.H.
A network of dynamically conserved residues deciphers the motions of maltose transporter
Proteins
76
588-597
2009
Escherichia coli (P68187), Escherichia coli
brenda
Li, M.; Chen, Z.; Zhang, X.; Song, Y.; Wen, Y.; Li, J.
Enhancement of avermectin and ivermectin production by overexpression of the maltose ATP-binding cassette transporter in Streptomyces avermitilis
Biores. Technol.
101
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2010
Streptomyces avermitilis, Streptomyces avermitilis ATCC 31267
brenda
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Alternating access in maltose transporter mediated by rigid-body rotations
Mol. Cell
33
528-536
2009
Escherichia coli (P68187)
brenda
Bordignon, E.; Grote, M.; Schneider, E.
The maltose ABC transporter in the 21(st) century - towards a structural-dynamic perspective on its mode of action
Mol. Microbiol.
77
1354-1366
2010
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P68187)
brenda
Gabrielsen, C.; Brede, D.; Hernandez, P.; Nes, I.; Diep, D.
The maltose ABC transporter in Lactococcus lactis facilitates high-level sensitivity to the circular bacteriocin garvicin ML
Antimicrob. Agents Chemother.
56
2908-2915
2012
Lactococcus lactis, Lactococcus lactis IL1403
brenda
Gould, A.; Shilton, B.
Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate
J. Biol. Chem.
285
11290-11296
2010
Escherichia coli
brenda
Cui, J.; Qasim, S.; Davidson, A.
Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter
J. Biol. Chem.
285
39986-39993
2010
Escherichia coli
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Jacso, T.; Schneider, E.; Rupp, B.; Reif, B.
Substrate transport activation is mediated through second periplasmic loop of transmembrane protein MalF in maltose transport complex of Escherichia coli
J. Biol. Chem.
287
17040-17049
2012
Escherichia coli
brenda
Bao, H.; Duong, F.
Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2
PLoS ONE
7
e34836
2012
Escherichia coli
brenda
Oldham, M.; Chen, J.
Crystal structure of the maltose transporter in a pretranslocation intermediate state
Science
332
1202-1205
2011
Escherichia coli
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Bao, H.; Dalal, K.; Wang, V.; Rouiller, I.; Duong, F.
The maltose ABC transporter: action of membrane lipids on the transporter stability, coupling and ATPase activity
Biochim. Biophys. Acta
1828
1723-1730
2013
Escherichia coli
brenda
Henrich, A.; Kuhlmann, N.; Eck, A.W.; Kraemer, R.; Seibold, G.M.
Maltose uptake by the novel ABC transport system MusEFGK2I causes increased expression of ptsG in Corynebacterium glutamicum
J. Bacteriol.
195
2573-2584
2013
Corynebacterium glutamicum (Q8NMV1), Corynebacterium glutamicum ATCC 13032 (Q8NMV1)
brenda
Alvarez, F.J.; Orelle, C.; Huang, Y.; Bajaj, R.; Everly, R.M.; Klug, C.S.; Davidson, A.L.
Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter
Mol. Microbiol.
98
878-894
2015
Escherichia coli (P68187), Escherichia coli
brenda
Chen, S.; Oldham, M.L.; Davidson, A.L.; Chen, J.
Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography
Nature
499
364-368
2013
Escherichia coli (P68187), Escherichia coli
brenda
Boehm, S.; Licht, A.; Wuttge, S.; Schneider, E.; Bordignon, E.
Conformational plasticity of the type I maltose ABC importer
Proc. Natl. Acad. Sci. USA
110
5492-5497
2013
Escherichia coli (P68187), Escherichia coli
brenda
Singh, R.; White, D.; Blum, P.
Identification of the ATPase subunit of the primary maltose transporter in the hyperthermophilic anaerobe Thermotoga maritima
Appl. Environ. Microbiol.
83
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2017
Thermotoga maritima (Q9X0S9 AND Q9X2F5), Thermotoga maritima
brenda
Wuttge, S.; Licht, A.; Timachi, M.H.; Bordignon, E.; Schneider, E.
Mode of interaction of the signal-transducing protein EIIA(Glc) with the maltose ABC transporter in the process of inducer exclusion
Biochemistry
55
5442-5452
2016
Escherichia coli
brenda
Bajaj, R.; Park, M.I.; Stauffacher, C.V.; Davidson, A.L.
Conformational dynamics in the binding-protein-independent mutant of the Escherichia coli maltose transporter, MalG511, and its interaction with maltose binding protein
Biochemistry
57
3003-3015
2018
Escherichia coli
brenda
Brickwedde, A.; Brouwers, N.; van den Broek, M.; Gallego Murillo, J.S.; Fraiture, J.L.; Pronk, J.T.; Daran, J.G.
Structural, physiological and regulatory analysis of maltose transporter genes in Saccharomyces eubayanus CBS 12357T
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Saccharomyces eubayanus, Saccharomyces eubayanus CBS 12357T
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Bao, H.; Dalal, K.; Cytrynbaum, E.; Duong, F.
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290
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Escherichia coli
brenda
Carlson, M.L.; Bao, H.; Duong, F.
Formation of a chloride-conducting state in the maltose ATP-binding cassette (ABC) transporter
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291
12119-12125
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Escherichia coli (P68187 and P68183 and P02916)
brenda
Hsu, W.L.; Furuta, T.; Sakurai, M.
Analysis of the free energy landscapes for the opening-closing dynamics of the maltose transporter ATPase MalK2 using enhanced-sampling molecular dynamics simulation
J. Phys. Chem. B
119
9717-9725
2015
Escherichia coli
brenda
Hsu, W.L.; Furuta, T.; Sakurai, M.
ATP hydrolysis mechanism in a maltose transporter explored by QM/MM metadynamics simulation
J. Phys. Chem. B
120
11102-11112
2016
Escherichia coli
brenda
Weng, J.; Gu, S.; Gao, X.; Huang, X.; Wang, W.
Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2
Phys. Chem. Chem. Phys.
19
9366-9373
2017
Escherichia coli
brenda
Lv, X.; Liu, H.; Chen, H.; Gong, H.
Coupling between ATP hydrolysis and protein conformational change in maltose transporter
Proteins
85
207-220
2017
Escherichia coli (P68187)
brenda
Hsu, W.L.; Furuta, T.; Sakurai, M.
The mechanism of nucleotide-binding domain dimerization in the intact maltose transporter as studied by all-atom molecular dynamics simulations
Proteins
86
237-247
2018
Escherichia coli (P68187 and P68183 and P02916 and P0AEX9), Escherichia coli
brenda
Licht, A.; Bommer, M.; Werther, T.; Neumann, K.; Hobe, C.; Schneider, E.
Structural and functional characterization of a maltose/maltodextrin ABC transporter comprising a single solute binding domain (MalE) fused to the transmembrane subunit MalF
Res. Microbiol.
170
1-12
2019
Bdellovibrio bacteriovorus (Q6MNM0), Bdellovibrio bacteriovorus, Bdellovibrio bacteriovorus HD100 (Q6MNM0)
brenda
Henderson, R.; Poolman, B.
Proton-solute coupling mechanism of the maltose transporter from Saccharomyces cerevisiae
Sci. Rep.
7
14375
2017
Saccharomyces cerevisiae, Saccharomyces cerevisiae IMK289
brenda