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PDBsum entry 1pyd
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Lyase(carbon-carbon)
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PDB id
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1pyd
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution.
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Authors
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F.Dyda,
W.Furey,
S.Swaminathan,
M.Sax,
B.Farrenkopf,
F.Jordan.
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Ref.
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Biochemistry, 1993,
32,
6165-6170.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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The crystal structure of brewers' yeast pyruvate decarboxylase, a thiamin
diphosphate dependent alpha-keto acid decarboxylase, has been determined to
2.4-A resolution. The homotetrameric assembly contains two dimers, exhibiting
strong intermonomer interactions within each dimer but more limited ones between
dimers. Each monomeric subunit is partitioned into three structural domains, all
folding according to a mixed alpha/beta motif. Two of these domains are
associated with cofactor binding, while the other is associated with substrate
activation. The catalytic centers containing both thiamin diphosphate and Mg(II)
are located deep in the intermonomer interface within each dimer. Amino acids
important in cofactor binding and likely to participate in catalysis and
substrate activation are identified.
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Secondary reference #1
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Title
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The DNA-Binding domain of the yeast saccharomyces cerevisiae cyp1(hap1) transcription factor possesses two zinc ions which are complexed in a zinc cluster.
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Authors
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J.E.Timmerman,
B.Guiard,
E.Shechter,
M.A.Delsuc,
J.Y.Lallemand,
M.Gervais.
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Ref.
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Eur J Biochem, 1994,
225,
593-599.
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PubMed id
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Secondary reference #2
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Title
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Preliminary crystallographic data for the thiamin diphosphate-Dependent enzyme pyruvate decarboxylase from brewers' Yeast.
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Authors
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F.Dyda,
W.Furey,
S.Swaminathan,
M.Sax,
B.Farrenkopf,
F.Jordan.
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Ref.
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J Biol Chem, 1990,
265,
17413-17415.
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PubMed id
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