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Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450BioI ACP complex

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Cryle,  Max
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Cytochrome P450, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Cryle, M., & Schlichting, I. (2008). Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450BioI ACP complex. Proceedings of the National Academy of Sciences of the United States of America, 105(41), 15696-15701. doi:10.1073/pnas.0805983105.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-5AA4-B
Abstract
Cytochrome P450BioI (CYP107H1) from the biotin operon of <i>Bacillus subtilis</i> forms a seven-carbon diacid through a multistep oxidative cleavage of a fatty acid linked to acyl carrier protein (ACP). Crystal structures of P450BioI in complex with three different length fatty <i>acyl</i>-ACP (<i>Escherichia coli</i>) ligands show that P450BioI 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 P450BioI-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.