1CJC

STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS

1CJC の概要

• エントリーDOI: 10.2210/pdb1cjc/pdb
• 分子名称: PROTEIN (ADRENODOXIN REDUCTASE), FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: flavoenzyme, mad analysis, electron transferase, oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51145.96

構造登録者

Ziegler, G.A.,Vonrhein, C.,Schulz, G.E. (登録日: 1999-04-12, 公開日: 1999-04-30, 最終更新日: 2023-12-27)

主引用文献

Ziegler, G.A.,Vonrhein, C.,Hanukoglu, I.,Schulz, G.E.
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis.
J.Mol.Biol., 289:981-990, 1999

PubMed Abstract: Adrenodoxin reductase is a monomeric 51 kDa flavoenzyme that is involved in the biosynthesis of all steroid hormones. The structure of the native bovine enzyme was determined at 2.8 A resolution, and the structure of the respective recombinant enzyme at 1.7 A resolution. Adrenodoxin reductase receives a two-electron package from NADPH and converts it to two single electrons that are transferred via adrenodoxin to all mitochondrial cytochromes P 450. The structure suggests how the observed flavin semiquinone is stabilized. A striking feature is the asymmetric charge distribution, which most likely controls the approach of the electron carrier adrenodoxin. A model for the interaction is proposed. Adrenodoxin reductase shows clear sequence homology to half a dozen proteins identified in genome analysis projects, but neither sequence nor structural homology to established, functionally related electron transferases. Yet, the structure revealed a relationship to the disulfide oxidoreductases, permitting the assignment of the NADP-binding site.

PubMed: 10369776
DOI: 10.1006/jmbi.1999.2807

実験手法

X-RAY DIFFRACTION (1.7 Å)