1MZO

Crystal structure of pyruvate formate-lyase with pyruvate

1MZO の概要

• エントリーDOI: 10.2210/pdb1mzo/pdb
• 分子名称: Pyruvate formate-lyase, TRIETHYLENE GLYCOL, PYRUVIC ACID, ... (4 entities in total)
• 機能のキーワード: enzyme-substrate complex, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P09373
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 170982.09

構造登録者

Lehtio, L.,Leppanen, V.-M.,Kozarich, J.W.,Goldman, A. (登録日: 2002-10-09, 公開日: 2002-12-11, 最終更新日: 2023-11-15)

主引用文献

Lehtio, L.,Leppanen, V.M.,Kozarich, J.W.,Goldman, A.
Structure of Escherichia coli pyruvate formate-lyase with pyruvate.
Acta Crystallogr.,Sect.D, 58:2209-2212, 2002

PubMed Abstract: The structure of inactive pyruvate formate-lyase in complex with a natural substrate, pyruvate, was solved at 2.7 A resolution. Both active sites of the homodimeric enzyme are occupied by pyruvate; additional binding sites were not found. Pyruvate was found in a cleft close to the active-site cysteines 418 and 419, with the carboxyl group in contact with arginines 176 and 435 and the methyl group within van der Waals distance of Phe327. It is believed that the binding site of pyruvate is not the position of pyruvate as the reaction initiates, as conformational changes occur during activation of the enzyme.

PubMed: 12454503
DOI: 10.1107/S0907444902016402

実験手法

X-RAY DIFFRACTION (2.7 Å)