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x * 59000, SDS-PAGE, recombinant protein
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x * 45953, recombinant 1-lip E2, mass spectrometry, x * 8982, recombinant unacetylated hybrid lipoyl domain, mass spectrometry, x * 9019, recombinant fully acetylated hybrid lipoyl domain, mass spectrometry
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x * 30028, catalytic domain, calculated from amino acid sequence
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x * 30030, catalytic domain, FT mass spectrometry
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x * 65959, calculated from amino acid sequence
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x * 33100, about, E2, sequence calculation
dimer
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multimer formation is probably lost by loss of a small segment during genetic rearrangement
dimer
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2 * 36000, in the presence of dilute acetic acid
dimer
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60mer, analytical ultracentrifugation
dimer
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GST-L2, glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase exists as a dimer
polymer
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polymer
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30 * 66000, SDS-PAGE, sedimentation equilibrium
polymer
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24 * 27500, SDS-PAGE, light scattering experiments, quarternary structure
polymer
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gel filtration in presence of guanidine-HCl, anomalous migration on SDS
polymer
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domain structure of subunits: lipoyl domain MW 28000, subunit binding domain MW 26000, sedimentation equilibrium
polymer
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30 * 70000, SDS-PAGE, each polypeptide chains has 2 domains
polymer
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24 * 36000, linked by noncovalent bonds
polymer
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24 * 40000, linked by noncovalent bonds
polymer
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22 or 24 subunits
polymer
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domain structure
polymer
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24 * 65959, calculation from nucleotide sequence
polymer
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24 identical subunits, data from crystallographic, biochemical and electron microscopic methods
polymer
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x * 46265, calculation from nucleotide sequence
polymer
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primary structure of lipoyl domain
polymer
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stoichiometry of pyruvate dehydrogenase complexes
polymer
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60 polypeptide chains, crystal structure
polymer
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60 * 42000, SDS-PAGE
polymer
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stoichiometry of pyruvate dehydrogenase complexes
polymer
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x * 48546, calculation from nucleotide sequence
polymer
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stoichiometry of pyruvate dehydrogenase complexes
polymer
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24 * 74000 SDS-PAGE, gel filtration in 6 M guanidine-HCl, sedimentation equilibrium in 6 M guanidine-HCl
polymer
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x * 60000, SDS-PAGE
polymer
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24 * 60000, SDS-PAGE
trimer
x-ray crystallography
trimer
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3 * 82000, gel filtration, trimeric form occurs in solutions with 4 M guanidine hydrochloride
additional information
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enzyme forms stable aggregates
additional information
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the enzyme forms the core unit of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its peripheral domain, Arg135 is important for interactions with E1 and E3, Met131 is involved in binding of E1, interaction analysis by surface plasmon resonance
additional information
cryoelectron microscopic analysis of the reconstructed three-dimensional structure of the purified E2E3 complex (dihydrolipoyl acetyltransferase/dihydrolipoyl dehydrogenase) and use of automated docking methods to interpret the density map in terms of the probable localization of the dihydrolipoyl acetyltransferase E2 and dihydrolipoyl dehydrogenase E3 molecules. The arrangement of pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3 molecules in the outer shell of the pyruvate dehydrogenase complex are remarkably similar and indicate that the design of the annular gap allows the lipoyl domain to have access to the active sites of pyruvate decarboxylase E1, dihydrolipoyl acetyltransferase E2, and dihydrolipoyl dehydrogenase E3 enzymes from within the annular gap
additional information
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cryoelectron microscopic analysis of the reconstructed three-dimensional structure of the purified E2E3 complex (dihydrolipoyl acetyltransferase/dihydrolipoyl dehydrogenase) and use of automated docking methods to interpret the density map in terms of the probable localization of the dihydrolipoyl acetyltransferase E2 and dihydrolipoyl dehydrogenase E3 molecules. The arrangement of pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3 molecules in the outer shell of the pyruvate dehydrogenase complex are remarkably similar and indicate that the design of the annular gap allows the lipoyl domain to have access to the active sites of pyruvate decarboxylase E1, dihydrolipoyl acetyltransferase E2, and dihydrolipoyl dehydrogenase E3 enzymes from within the annular gap
additional information
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distinct modes of recognition of the lipoyl domain of the dihydrolipoyl acetyltransferase (E2) component as substrate by the E1 and E3 components of the pyruvate dehydrogenase multienzyme complex
additional information
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E2 is composed of 4 domains including the innerlipoyl domain L2 important for binding of E1
additional information
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enzyme is a 60mer, E2 domain structure: 4 domains, i.e. L1, L2, B, and I domain, connected by linker oligomers, overview, overall multienzyme complex organization, overview
additional information
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the enzyme forms the core unit E2, consisting of 4 domains in 60mer, a trimer of 3 20mers, of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase and dihydrolipoyl dehydrogenase, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview
additional information
evidence for a novel subunit organization in which dihydrolipoamide dehydrogenase E3 and E3BP form subcomplexes with a 1:2 stoichiometry implying the existence of a network of dihydrolipoamide dehydrogenase cross-bridges linking pairs of E3-binding proteins across the surface of the dihydrolipoamide acetyltransferase E2 core assembly. One of the E3-binding protein lipoyl domains docks into the dihydrolipoamide dehydrogenase E3 active site
additional information
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enzyme is a 60mer, E2 domain structure: 4 domains, i.e. L1, L2, B, and I domain, connected by linker oligomers, overview, overall multienzyme complex organization, overview
additional information
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the enzyme forms the core unit E2, consisting of 4 domains in 60mer, a trimer of 3 20mers, of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase and dihydrolipoyl dehydrogenase, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview
additional information
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treatment with NaCl results in 2 fractions with E2 activity, MW 55000 and MW 78000, SDS-PAGE, gel filtration