2VJY

Pyruvate decarboxylase from Kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate

2VJY の概要

• エントリーDOI: 10.2210/pdb2vjy/pdb
• 関連するPDBエントリー: 2G1I 2VK4
• 分子名称: PYRUVATE DECARBOXYLASE, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: metal-binding, decarboxylase, dimer of dimers, methylacetylphosphonate, methyl acetylphosphonate, substrate activation, thiamine diphosphate, thiamine pyrophosphate, asymmetric active sites, map, lyase, pyruvate, magnesium, flavoprotein
• 由来する生物種: KLUYVEROMYCES LACTIS (YEAST)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 250200.30

構造登録者

Kutter, S.,Wille, G.,Weiss, M.S.,Konig, S. (登録日: 2007-12-14, 公開日: 2009-01-27, 最終更新日: 2024-10-23)

主引用文献

Kutter, S.,Weiss, M.S.,Wille, G.,Golbik, R.,Spinka, M.,Konig, S.
Covalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation.
J.Biol.Chem., 284:12136-, 2009

PubMed Abstract: The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast species, three of them reported here for the first time, provide detailed atomic resolution snapshots along the activation coordinate. The prime event is the covalent binding of the substrate pyruvate to the side chain of cysteine 221, thus forming a thiohemiketal. This reaction causes the shift of a neighboring amino acid, which eventually leads to the rigidification of two otherwise flexible loops, one of which provides two histidine residues necessary to complete the enzymatically competent active site architecture. The structural data are complemented and supported by kinetic investigations and binding studies, providing a consistent picture of the structural changes occurring upon enzyme activation.

PubMed: 19246454
DOI: 10.1074/JBC.M806228200

実験手法

X-RAY DIFFRACTION (2.3 Å)