3WKT

Complex structure of an open form of NADPH-cytochrome P450 reductase and heme oxygenase-1

3WKT の概要

• エントリーDOI: 10.2210/pdb3wkt/pdb
• 分子名称: NADPH-cytochrome P450 reductase, Heme oxygenase 1, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: heme degradation, microsomal membrane, oxidoreductase
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats); 詳細
• 細胞内の位置: Endoplasmic reticulum membrane ; Single-pass membrane protein ; Cytoplasmic side : P00388; Microsome: P06762
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 206992.77

構造登録者

Sugishima, M.,Sato, H.,Higashimoto, Y.,Harada, J.,Wada, K.,Fukuyama, K.,Noguchi, M. (登録日: 2013-10-31, 公開日: 2014-01-29, 最終更新日: 2023-11-08)

主引用文献

Sugishima, M.,Sato, H.,Higashimoto, Y.,Harada, J.,Wada, K.,Fukuyama, K.,Noguchi, M.
Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.
Proc.Natl.Acad.Sci.USA, 111:2524-2529, 2014

PubMed Abstract: NADPH-cytochrome P450 oxidoreductase (CPR) supplies electrons to various heme proteins including heme oxygenase (HO), which is a key enzyme for heme degradation. Electrons from NADPH flow first to flavin adenine dinucleotide, then to flavin mononucleotide (FMN), and finally to heme in the redox partner. For electron transfer from CPR to its redox partner, the ''closed-open transition'' of CPR is indispensable. Here, we demonstrate that a hinge-shortened CPR variant, which favors an open conformation, makes a stable complex with heme-HO-1 and can support the HO reaction, although its efficiency is extremely limited. Furthermore, we determined the crystal structure of the CPR variant in complex with heme-HO-1 at 4.3-Å resolution. The crystal structure of a complex of CPR and its redox partner was previously unidentified. The distance between heme and FMN in this complex (6 Å) implies direct electron transfer from FMN to heme.

PubMed: 24550278
DOI: 10.1073/pnas.1322034111

実験手法

X-RAY DIFFRACTION (4.3 Å)