1PYD

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

1PYD の概要

• エントリーDOI: 10.2210/pdb1pyd/pdb
• 分子名称: PYRUVATE DECARBOXYLASE, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: lyase(carbon-carbon)
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122643.93

構造登録者

Furey, W.,Dyda, F. (登録日: 1993-03-23, 公開日: 1994-04-30, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)