1PYD

CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE DECARBOXYLASE AT 2.4 ANGSTROMS RESOLUTION

Summary for 1PYD

• Entry DOI: 10.2210/pdb1pyd/pdb
• Descriptor: PYRUVATE DECARBOXYLASE, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: lyase(carbon-carbon)
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 122643.93

Authors

Furey, W.,Dyda, F. (deposition date: 1993-03-23, release date: 1994-04-30, Last modification date: 2024-02-14)

Primary citation

Dyda, F.,Furey, W.,Swaminathan, S.,Sax, M.,Farrenkopf, B.,Jordan, F.
Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution.
Biochemistry, 32:6165-6170, 1993

PubMed Abstract: 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.

PubMed: 8512926
DOI: 10.1021/bi00075a008

Experimental method

X-RAY DIFFRACTION (2.4 Å)