1BU7

CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN

1BU7 の概要

• エントリーDOI: 10.2210/pdb1bu7/pdb
• 分子名称: PROTEIN (CYTOCHROME P450), PROTOPORPHYRIN IX CONTAINING FE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: fatty acid monooxygenase, hemoprotein, p450, oxidoreductase
• 由来する生物種: Bacillus megaterium
• 細胞内の位置: Cytoplasm (By similarity): P14779
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106440.85

構造登録者

Li, H.,Poulos, T.L. (登録日: 1998-09-14, 公開日: 1998-09-23, 最終更新日: 2024-02-07)

主引用文献

Sevrioukova, I.F.,Li, H.,Zhang, H.,Peterson, J.A.,Poulos, T.L.
Structure of a cytochrome P450-redox partner electron-transfer complex.
Proc.Natl.Acad.Sci.USA, 96:1863-1868, 1999

PubMed Abstract: The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450.

PubMed: 10051560
DOI: 10.1073/pnas.96.5.1863

実験手法

X-RAY DIFFRACTION (1.65 Å)