1cjc
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STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS
OverviewOverview
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.
About this StructureAbout this Structure
1CJC is a Single protein structure of sequence from Bos taurus with FAD as ligand. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Full crystallographic information is available from OCA.
ReferenceReference
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis., Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE, J Mol Biol. 1999 Jun 18;289(4):981-90. PMID:10369776
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