1bu7: Difference between revisions

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[[Image:1bu7.gif|left|200px]]
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{{STRUCTURE_1bu7|  PDB=1bu7  |  SCENE=  }}  
{{STRUCTURE_1bu7|  PDB=1bu7  |  SCENE=  }}  


'''CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN'''
===CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN===




==Overview==
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The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450.
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==About this Structure==
==About this Structure==
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[[Category: Hemoprotein]]
[[Category: Hemoprotein]]
[[Category: P450]]
[[Category: P450]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:43:44 2008''

Revision as of 19:43, 30 June 2008

File:1bu7.png

Template:STRUCTURE 1bu7

CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAINCRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN

Template:ABSTRACT PUBMED 10051560

About this StructureAbout this Structure

1BU7 is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a cytochrome P450-redox partner electron-transfer complex., Sevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL, Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1863-8. PMID:10051560

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