2zwt

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Crystal Structure of Ferric Cytochrome P450camCrystal Structure of Ferric Cytochrome P450cam

Structural highlights

2zwt is a 1 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:, , ,
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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Sakurai K, Shimada H, Hayashi T, Tsukihara T. Substrate binding induces structural changes in cytochrome P450cam. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt, 2):80-3. Epub 2009 Jan 31. PMID:19193991 doi:10.1107/S1744309108044114

2zwt, resolution 1.35Å

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