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1.14.99.54: lytic cellulose monooxygenase (C1-hydroxylating)

This is an abbreviated version!
For detailed information about lytic cellulose monooxygenase (C1-hydroxylating), go to the full flat file.

Word Map on EC 1.14.99.54

Reaction

[(1->4)-beta-D-glucosyl]n+m
+
reduced acceptor
 +
O2
=
[(1->4)-beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone
 +
[(1->4)-beta-D-glucosyl]n
 +
acceptor
 +
H2O

Synonyms

AA13, AA14A, AA14B, AA9, AA9 LPMO, AA9A, AO090701000246, CBP21, Cel61a, cel61b, Cel7A, CelS2, chitin-binding domain 3 protein, endoglucanase II, endoglucanase IV, FG02202.1, GbpA, Gh61 isozyme a, gh61-4, gh61-5, GH61D, gh61e, GH61H, LPMO, LPMO-02916, LPMO10A, LPMO10B, LPMO10C, LPMO9A, LPMO9B, LPMO9C, LPMO9D, LPMO9E, LPMO9f, Lpmo9H, lytic polysaccharide monooxygenase, Micau_1630, NCU01050, NCU07898, PaGH61A, PaGH61B, PMO, PMO-2, PMO-3, PODANS_2_6530, PODANS_7_3160, polysaccharide monoxygenase, PsLPMOA, PsLPMOB, Pte6, SCO0643, SCO1188, Tfu_1268, Tfu_1665

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.54 lytic cellulose monooxygenase (C1-hydroxylating)

Crystallization

Crystallization on EC 1.14.99.54 - lytic cellulose monooxygenase (C1-hydroxylating)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals obtained in the presence of high zinc-ion concentrations are used. A structure with an ordered zinc-bound active site at 1.65 A resolution, and three structures from crystals soaked with maltooligosaccharides in solutions devoid of zinc ions are solved at resolutions of up to 1.10 A
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
1.2 A resolution X-ray diffraction data, room-temperature neutron diffraction data to 2.12 A resolution
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues
comparison of isoforms PMO-2 and PMO-3 at 1.1 and 1.37 resolution, respectively. In the structures, dioxygen species are found in the active sites. The enzyme substrate-binding surfaces contain highly varied aromatic amino acid and glycosylation positions
single-molecule study by atomic force microscopy
-
to 1.2 A resolution, P21 space group with two protein molecules with non-crystallographic symmetry per asymmetric unit. Role for a conserved histidine in promoting oxygen activation
structure determined at pH 3.5, shows significant disorder of the active site in the absence of substrate ligand
structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides
to 1.75 A resolution. Stucture reveals a copper-bound active site common to LPMOs, a collection of aromatic and polar residues near the binding surface that may be responsible for regioselectivity, and substantial differences in loop structures near the binding face. Surface analysis reveals energy wells whose spacing seems adapted to the spacing of cellobiose units along a cellulose chain
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues
hybrid quantum mechanics and molecular mechanics investigation of the first steps of the LPMO mechanism, which is reduction of CuII to CuI and the formation of a CuII-superoxide complex. In the complex, the superoxide can bind either in an equatorial or an axial position. The equatorial isomer of the superoxide complex is over 60 kJ/mol more stable than the axial isomer because it is stabilized by interactions with a second-coordination-sphere glutamine residue
comparison of isoforms LPMO9A, LPMO9B and LPMO9C. LPMO9B contains distal from the coordinated copper sphere an additional loop (Gly115-Asn121), which is not present in LPMO9A and LPMO9C. The copper ion in LPMO9A, LPMO9B and LPMO9C is coordinated by His1-His68-Tyr153, His1-His79-Tyr170 and His1-His84-Tyr166, respectively. All three LPMOs share two putative disulfide bridges
modeling of structure. The divalent metal ion in the active site is coordinated by the three amino acids, His1, His68 and Tyr153. LPMO9A comprises two disulfide bridges, Cys126-Cys208 and Cys38-Cys156
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues
to 3.0 A resolution. The active site of AA14B is constituted by His1, His99 and Tyr176, forming the canonical histidine brace that is exposed at the surface
C-terminally truncated variant containing 21 residues of the predicted linker domain, to 0.95 A resolution. The linker forms an integral part of the catalytic domain structure, covering a hydrophobic patch on the catalytic AA9 module. The oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand
comparative analysis of sequences, solved structures, and homology models from AA9 and AA10 LPMO families.The two LPMO families are highly conserved, structurally they have minimal sequence similarity outside the active site residues