1oxa: Difference between revisions

Revision as of 04:23, 3 May 2008

CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)

OverviewOverview

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 StructureAbout this Structure

1OXA is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

ReferenceReference

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 Sat May 3 04:23:26 2008

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OCA

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 [[Image:1oxa.jpg|left|200px]]
- {{Structure
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-}}
 '''CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)'''
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 [[Category: Cupp-Vickery, J R.]]
 [[Category: Poulos, T L.]]
-[[Category: oxidoreductase (oxygenase)]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:23:26 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:40 2008''