3EJE

Crystal Structure of P450BioI in complex with octadec-9Z-enoic acid ligated Acyl Carrier Protein

Summary for 3EJE

• Entry DOI: 10.2210/pdb3eje/pdb
• Related: 3EJB 3EJD
• Descriptor: Acyl carrier protein, Biotin biosynthesis cytochrome P450-like enzyme, S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] (9Z)-octadec-9-enethioate, ... (6 entities in total)
• Functional Keywords: protein-protein complex, cytochrome p450 fold, carrier protein, 4-helix bundle, fatty acid biosynthesis, lipid synthesis, phosphopantetheine, biotin biosynthesis, heme, iron, metal-binding, monooxygenase, oxidoreductase, oxidoreductase-lipid transport complex, oxidoreductase/lipid transport
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A6A8
• Total number of polymer chains: 8
• Total formula weight: 233713.91

Authors

Cryle, M.J.,Schlichting, I. (deposition date: 2008-09-18, release date: 2008-10-07, Last modification date: 2024-10-30)

Primary citation

Cryle, M.J.,Schlichting, I.
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
Proc.Natl.Acad.Sci.Usa, 105:15696-15701, 2008

PubMed 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.

PubMed: 18838690
DOI: 10.1073/pnas.0805983105

Experimental method

X-RAY DIFFRACTION (2.1 Å)