3ejb

Crystal Structure of P450BioI in complex with tetradecanoic acid ligated Acyl Carrier Protein

spinqualitylabelsall models 3ejb, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ejb is a 8 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900 and Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, HEM, HTG, ZMP Related: 3ejd, 3eje Gene: acpP, b1094, JW1080 (ECOLI), bioI, CYP107H, BSU30190 ("Bacillus globigii" Migula 1900) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACP_ECOLI] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] [BIOI_BACSU] Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.,Cryle MJ, Schlichting I Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15696-701. Epub 2008 Oct 6. PMID:18838690 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein Fatty acid synthase

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