2ZWU

Crystal Structure of Camphor Soaked Ferric Cytochrome P450cam

2ZWU の概要

• エントリーDOI: 10.2210/pdb2zwu/pdb
• 関連するPDBエントリー: 2CPP 2ZAX 2ZWT
• 分子名称: Camphor 5-monooxygenase, PROTOPORPHYRIN IX CONTAINING FE, CAMPHOR, ... (6 entities in total)
• 機能のキーワード: p450cam, monooxygenase, camphor-hydroxylase, heme, iron, metal-binding, oxidoreductase, substrate-soaking, cytoplasm
• 由来する生物種: Pseudomonas Putida
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47650.03

構造登録者

Sakurai, K.,Shimada, H.,Hayashi, T.,Tsukihara, T. (登録日: 2008-12-18, 公開日: 2009-02-17, 最終更新日: 2023-11-01)

主引用文献

Sakurai, K.,Shimada, H.,Hayashi, T.,Tsukihara, T.
Substrate binding induces structural changes in cytochrome P450cam
Acta Crystallogr.,Sect.F, 65:80-83, 2009

PubMed Abstract: The binding of (+)-camphor to cytochrome P450cam (P450cam) expels a cluster of waters at the active site, raising the redox potential of the haem to an extent that allows reduction by the electron-transfer system. This binding was reported to involve no significant structural changes in the protein. Here, two ferric P450cam structures partially complexed with (+)-camphor were determined by X-ray crystallography at 1.30-1.35 A resolution, revealing the structures of the substrate-free and substrate-bound forms. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to the redox-potential change.

PubMed: 19193991
DOI: 10.1107/S1744309108044114

実験手法

X-RAY DIFFRACTION (1.3 Å)