1CJC

STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS

Summary for 1CJC

• Entry DOI: 10.2210/pdb1cjc/pdb
• Descriptor: PROTEIN (ADRENODOXIN REDUCTASE), FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: flavoenzyme, mad analysis, electron transferase, oxidoreductase
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 51145.96

Authors

Ziegler, G.A.,Vonrhein, C.,Schulz, G.E. (deposition date: 1999-04-12, release date: 1999-04-30, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)