3FJO

Structure of chimeric YH CPR

3FJO の概要

• エントリーDOI: 10.2210/pdb3fjo/pdb
• 関連するPDBエントリー: 1AMO 2BF4
• 分子名称: NADPH-cytochrome P450 reductase, FLAVIN MONONUCLEOTIDE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: fmn and fad domains of cpr, oxidoreductase, endoplasmic reticulum, flavoprotein, membrane, nadp, phosphoprotein, transmembrane, congenital adrenal hyperplasia, disease mutation
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast, Human); 詳細
• 細胞内の位置: Endoplasmic reticulum membrane ; Single-pass membrane protein ; Cytoplasmic side : P16435
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 72661.22

構造登録者

Morera, S.,Aigrain, L.,Truan, G. (登録日: 2008-12-15, 公開日: 2009-06-16, 最終更新日: 2023-11-01)

主引用文献

Aigrain, L.,Pompon, D.,Morera, S.,Truan, G.
Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase
Embo Rep., 10:742-747, 2009

PubMed Abstract: Two catalytic domains, bearing FMN and FAD cofactors, joined by a connecting domain, compose the core of the NADPH cytochrome P450 reductase (CPR). The FMN domain of CPR mediates electron shuttling from the FAD domain to cytochromes P450. Together, both enzymes form the main mixed-function oxidase system that participates in the metabolism of endo- and xenobiotic compounds in mammals. Available CPR structures show a closed conformation, with the two cofactors in tight proximity, which is consistent with FAD-to-FMN, but not FMN-to-P450, electron transfer. Here, we report the 2.5 A resolution crystal structure of a functionally competent yeast-human chimeric CPR in an open conformation, compatible with FMN-to-P450 electron transfer. Comparison with closed structures shows a major conformational change separating the FMN and FAD cofactors from 86 A.

PubMed: 19483672
DOI: 10.1038/embor.2009.82

実験手法

X-RAY DIFFRACTION (2.5 Å)