1F24
CRYSTAL STRUCTURE OF NO COMPLEX OF THR243ALA MUTANTS OF CYTOCHROME P450NOR
Summary for 1F24
| Entry DOI | 10.2210/pdb1f24/pdb |
| Related | 1F25 1F26 |
| Descriptor | NITRIC OXIDE REDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, NITRIC OXIDE, ... (5 entities in total) |
| Functional Keywords | nitric oxide reductase, cytochrome p450nor, oxidoreductase |
| Biological source | Fusarium oxysporum |
| Total number of polymer chains | 1 |
| Total formula weight | 44998.06 |
| Authors | Shimizu, H.,Park, S.-Y. (deposition date: 2000-05-23, release date: 2000-11-23, Last modification date: 2024-05-29) |
| Primary citation | Obayashi, E.,Shimizu, H.,Park, S.Y.,Shoun, H.,Shiro, Y. Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function. J.Inorg.Biochem., 82:103-111, 2000 Cited by PubMed Abstract: Threonine 243 of cytochrome P450nor (fungal nitric oxide reductase) corresponds to the 'conserved' Thr in the long I helix of monooxygenase cytochrome P450s. In P450nor, the replacement of Thr243 with Asn, Ala or Val makes the enzymatic activity dramatically reduce. In order to understand the roles of Thr243 in the reduction reaction of NO by P450nor, the crystal structures of three Thr243 mutants (Thr243-->Asn, Thr243-->Val, Thr243-->Ala) of P450nor were determined at a 1.4-A resolution and at cryogenic temperature. However, the hydrogen-bonding pattern in the heme pocket of these mutants is essentially similar for that of the WT enzyme. This suggests that the determination of the structure of the NADH complex of P450nor is required, in order to evaluate the role of Thr243 in its enzymatic reaction. We attempted to crystallize the NADH complex under several conditions, but have not yet been successful. PubMed: 11132616DOI: 10.1016/S0162-0134(00)00161-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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