2WVA

Structural insights into the pre-reaction state of pyruvate decarboxylase from Zymomonas mobilis

2WVA の概要

• エントリーDOI: 10.2210/pdb2wva/pdb
• 関連するPDBエントリー: 1ZPD 2WVG 2WVH
• 分子名称: PYRUVATE DECARBOXYLASE, 2-{1-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-METHYL-1H-1,2,3-TRIAZOL-4-YL}ETHYL TRIHYDROGEN DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: thiamin diphosphate, lyase, flavoprotein, metal-binding, alcohol fermentation
• 由来する生物種: ZYMOMONAS MOBILIS
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 491647.20

構造登録者

Pei, X.Y.,Erixon, K.,Luisi, B.F.,Leeper, F.J. (登録日: 2009-10-15, 公開日: 2010-02-09, 最終更新日: 2023-12-20)

主引用文献

Pei, X.Y.,Erixon, K.,Luisi, B.F.,Leeper, F.J.
Structural Insights Into the Pre-Reaction State of Pyruvate Decarboxylase from Zymomonas Mobilis
Biochemistry, 49:1727-, 2010

PubMed Abstract: Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the enzyme with pyruvate and a stable analogue of the cofactor's activated ylid form. A second crystal structure of PDC in complex with fluoride shows that the ion organizes a water molecule that occludes the pyruvate binding site, accounting for the inhibitory effect of the halide. Also reported is a structure of the cofactor-free apo form, which when compared to the structure of the holo form indicates how thiamine diphosphate organizes the active site pocket of pyruvate decarboxylase to support catalysis. Guided by the structural and enzymatic data, we propose roles for several key residues in the catalytic mechanism.

PubMed: 20099870
DOI: 10.1021/BI901864J

実験手法

X-RAY DIFFRACTION (2.2 Å)