1bu7
CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
|
OverviewOverview
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.
About this StructureAbout this Structure
1BU7 is a Single protein structure of sequence from Bacillus megaterium with HEM and EDO as ligands. Active as Unspecific monooxygenase, with EC number 1.14.14.1 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
Page seeded by OCA on Tue Nov 20 11:55:32 2007