1oxa
From Proteopedia
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CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)
Overview
Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several alpha-helices. The largest difference occurs in the B' helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction.
About this Structure
1OXA is a Single protein structure of sequence from Saccharopolyspora erythraea with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of cytochrome P450eryF involved in erythromycin biosynthesis., Cupp-Vickery JR, Poulos TL, Nat Struct Biol. 1995 Feb;2(2):144-53. PMID:7749919
Page seeded by OCA on Thu Feb 21 14:22:42 2008
