1cjc: Difference between revisions

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[[Image:1cjc.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1cjc|  PDB=1cjc  |  SCENE=  }}  
{{STRUCTURE_1cjc|  PDB=1cjc  |  SCENE=  }}  


'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''
===STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Flavoenzyme]]
[[Category: Flavoenzyme]]
[[Category: Mad analysis]]
[[Category: Mad analysis]]
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