2ZWT
Crystal Structure of Ferric Cytochrome P450cam
Summary for 2ZWT
| Entry DOI | 10.2210/pdb2zwt/pdb |
| Related | 2CPP 2ZAX 2ZWU |
| Descriptor | Camphor 5-monooxygenase, PROTOPORPHYRIN IX CONTAINING FE, CAMPHOR, ... (6 entities in total) |
| Functional Keywords | p450cam, monooxygenase, camphor-hydroxylase, heme, iron, metal-binding, oxidoreductase, cytoplasm |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 1 |
| Total formula weight | 47650.03 |
| Authors | Sakurai, K.,Shimada, H.,Hayashi, T.,Tsukihara, T. (deposition date: 2008-12-18, release date: 2009-02-17, Last modification date: 2023-11-01) |
| Primary citation | Sakurai, K.,Shimada, H.,Hayashi, T.,Tsukihara, T. Substrate binding induces structural changes in cytochrome P450cam Acta Crystallogr.,Sect.F, 65:80-83, 2009 Cited by PubMed Abstract: 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. PubMed: 19193991DOI: 10.1107/S1744309108044114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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