Abstract:
:Cytochrome P450(BioI) (CYP107H1) from the biotin operon of Bacillus subtilis forms a seven-carbon diacid through a multistep oxidative cleavage of a fatty acid linked to acyl carrier protein (ACP). Crystal structures of P450(BioI) in complex with three different length fatty acyl-ACP (Escherichia coli) ligands show that P450(BioI) binds the fatty acid such as to force the carbon chain into a U-shape above the active site heme. This positions the C7 and C8 carbons for oxidation, with a large additional cavity extending beyond the heme to accommodate the methyl termini of fatty acids beyond the site of cleavage. The structures explain the experimentally observed lack of stereo- and regiospecificity in the hydroxylation and cleavage of free fatty acids. The P450(BioI)-ACP complexes represent the only structurally characterized P450-carrier protein complexes to date, which has allowed the generation of a model of the interaction of the vancomycin biosynthetic P450 OxyB with its proposed carrier protein bound substrate.
journal_name
Proc Natl Acad Sci U S Aauthors
Cryle MJ,Schlichting Idoi
10.1073/pnas.0805983105subject
Has Abstractpub_date
2008-10-14 00:00:00pages
15696-701issue
41eissn
0027-8424issn
1091-6490pii
0805983105journal_volume
105pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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