2zwt

Crystal Structure of Ferric Cytochrome P450cam

spinqualitylabelsall models 2zwt, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zwt is a 1 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CAM, HEM, K, TRS Related: 2zwu, 2zax, 2cpp Gene: camC ("Bacillus fluorescens putidus" Flugge 1886) Activity: Camphor 5-monooxygenase, with EC number 1.14.15.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CPXA_PSEPU] Involved in a camphor oxidation system. 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 The binding of (+)-camphor to cytochrome P450cam (P450cam) expels a cluster of waters at the active site, raising the redox potential of the haem to an extent that allows reduction by the electron-transfer system. This binding was reported to involve no significant structural changes in the protein. Here, two ferric P450cam structures partially complexed with (+)-camphor were determined by X-ray crystallography at 1.30-1.35 A resolution, revealing the structures of the substrate-free and substrate-bound forms. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to the redox-potential change. Substrate binding induces structural changes in cytochrome P450cam.,Sakurai K, Shimada H, Hayashi T, Tsukihara T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt, 2):80-3. Epub 2009 Jan 31. PMID:19193991 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450

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