1cjc: Difference between revisions

Revision as of 20:49, 30 June 2008

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File:1cjc.png

Template:STRUCTURE 1cjc

STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMSSTRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS

Template:ABSTRACT PUBMED 10369776

About this StructureAbout this Structure

1CJC is a Single protein structure of sequence from Bos taurus. 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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-'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''
+===STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10369776}}, adds the Publication Abstract to the page
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 [[Category: Flavoenzyme]]
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