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2BN4

A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductase

2BN4 の概要
エントリーDOI10.2210/pdb2bn4/pdb
関連するPDBエントリー2BF4
分子名称NADPH CYTOCHROME P450 REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, FLAVIN MONONUCLEOTIDE, ... (5 entities in total)
機能のキーワードoxidoreductase, diflavin reductase, cpr, electron transfer, fmn-binding, fad, flavoprotein, nadph, oxidoreductase.
由来する生物種SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
タンパク質・核酸の鎖数2
化学式量合計155656.69
構造登録者
Podust, L.M.,Lepesheva, G.I.,Kim, Y.,Yermalitskaya, L.V.,Yermalitsky, V.N.,Lamb, D.C.,Kelly, S.L.,Waterman, M.R. (登録日: 2005-03-18, 公開日: 2006-01-17, 最終更新日: 2023-12-13)
主引用文献Lamb, D.C.,Kim, Y.,Yermalitskaya, L.V.,Yermalitsky, V.N.,Lepesheva, G.I.,Kelly, S.L.,Waterman, M.R.,Podust, L.M.
A Second Fmn-Binding Site in Yeast Nadph-Cytochrome P450 Reductase Suggests a Mechanism of Electron Transfer by Diflavin Reductases.
Structure, 14:51-, 2006
Cited by
PubMed Abstract: NADPH-cytochrome P450 reductase transfers two reducing equivalents derived from a hydride ion of NADPH via FAD and FMN to the large family of microsomal cytochrome P450 monooxygenases in one-electron transfer steps. The mechanism of electron transfer by diflavin reductases remains elusive and controversial. Here, we determined the crystal structure of truncated yeast NADPH-cytochrome P450 reductase, which is functionally active toward its physiological substrate cytochrome P450, and discovered a second FMN binding site at the interface of the connecting and FMN binding domains. The two FMN binding sites have different accessibilities to the bulk solvent and different amino acid environments, suggesting stabilization of different electronic structures of the reduced flavin. Since only one FMN cofactor is required for function, a hypothetical mechanism of electron transfer is discussed that proposes shuttling of a single FMN between these two sites coupled with the transition between two semiquinone forms, neutral (blue) and anionic (red).
PubMed: 16407065
DOI: 10.1016/J.STR.2005.09.015
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.91 Å)
構造検証レポート
Validation report summary of 2bn4
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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