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| [[Image:1cjc.gif|left|200px]] | | {{Seed}} |
| | [[Image:1cjc.png|left|200px]] |
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| {{STRUCTURE_1cjc| PDB=1cjc | SCENE= }} | | {{STRUCTURE_1cjc| PDB=1cjc | SCENE= }} |
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| '''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''
| | ===STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10369776}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10369776 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10369776}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Flavoenzyme]] | | [[Category: Flavoenzyme]] |
| [[Category: Mad analysis]] | | [[Category: Mad analysis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:47:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:49:42 2008'' |