1H17

Pyruvate Formate-Lyase (E.coli) in complex with CoA and the substrate analog oxamate

1H17 の概要

• エントリーDOI: 10.2210/pdb1h17/pdb
• 関連するPDBエントリー: 1CM5 1H16 1H18 1QHM 2PFL 3PFL
• 分子名称: FORMATE ACETYLTRANSFERASE 1, COENZYME A, OXAMIC ACID, ... (8 entities in total)
• 機能のキーワード: lyase, glycyl radical enzyme, transferase, acyltransferase acetylation
• 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: 1
• 化学式量合計: 87196.63

構造登録者

Becker, A.,Kabsch, W. (登録日: 2002-07-03, 公開日: 2002-11-01, 最終更新日: 2023-12-13)

主引用文献

Becker, A.,Kabsch, W.
X-Ray Structure of Pyruvate Formate-Lyase in Complex with Pyruvate and Coa.How the Enzyme Uses the Cys-418 Thiyl Radical for Pyruvate Cleavage
J.Biol.Chem., 277:40036-, 2002

PubMed Abstract: The glycyl radical enzyme pyruvate formate-lyase (PFL) synthesizes acetyl-CoA and formate from pyruvate and CoA. With the crystal structure of the non-radical form of PFL in complex with its two substrates, we have trapped the moment prior to pyruvate cleavage. The structure reveals how the active site aligns the scissile bond of pyruvate for radical attack, prevents non-radical side reactions of the pyruvate, and confines radical migration. The structure shows CoA in a syn conformation awaiting pyruvate cleavage. By changing to an anti conformation, without affecting the adenine binding mode of CoA, the thiol of CoA could pick up the acetyl group resulting from pyruvate cleavage.

PubMed: 12163496
DOI: 10.1074/JBC.M205821200

実験手法

X-RAY DIFFRACTION (1.75 Å)