Summary for 2XFH
| Entry DOI | 10.2210/pdb2xfh/pdb |
| Related | 2JJN 2JJO 2JJP 2VRV 2WIO |
| Descriptor | ERYTHROMYCIN B/D C-12 HYDROXYLASE, PROTOPORPHYRIN IX CONTAINING FE, 1-[(2-CHLOROPHENYL)(DIPHENYL)METHYL]-1H-IMIDAZOLE, ... (5 entities in total) |
| Functional Keywords | monoxygenase, erythromycin a biosynthesis, oxidoreductase |
| Biological source | SACCHAROPOLYSPORA ERYTHRAEA |
| Total number of polymer chains | 1 |
| Total formula weight | 46731.33 |
| Authors | Savino, C.,Montemiglio, L.C.,Gianni, S.,Vallone, B. (deposition date: 2010-05-24, release date: 2010-09-29, Last modification date: 2023-12-20) |
| Primary citation | Montemiglio, L.C.,Gianni, S.,Vallone, B.,Savino, C. Azole Drugs Trap Cytochrome P450 Eryk in Alternative Conformational States. Biochemistry, 49:9199-, 2010 Cited by PubMed Abstract: EryK is a bacterial cytochrome P450 that catalyzes the last hydroxylation occurring during the biosynthetic pathway of erythromycin A in Streptomyces erythraeus. We report the crystal structures of EryK in complex with two widely used azole inhibitors: ketoconazole and clotrimazole. Both of these ligands use their imidazole moiety to coordinate the heme iron of P450s. Nevertheless, because of the different chemical and structural properties of their N1-substituent group, ketoconazole and clotrimazole trap EryK, respectively, in a closed and in an open conformation that resemble the two structures previously described for the ligand-free EryK. Indeed, ligands induce a distortion of the internal helix I that affects the accessibility of the binding pocket by regulating the kink of the external helix G via a network of interactions that involves helix F. The data presented thus constitute an example of how a cytochrome P450 may be selectively trapped in different conformational states by inhibitors. PubMed: 20845962DOI: 10.1021/BI101062V PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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