1oxa
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(New page: 200px<br /><applet load="1oxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxa, resolution 2.1Å" /> '''CYTOCHROME P450 (DONO...)
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Revision as of 21:09, 20 November 2007
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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 HEM and DEB 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
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