2AHJ
NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE
Summary for 2AHJ
| Entry DOI | 10.2210/pdb2ahj/pdb |
| Descriptor | NITRILE HYDRATASE, FE (III) ION, ZINC ION, ... (8 entities in total) |
| Functional Keywords | lyase, photoreactive enzyme, nitric oxide binding enzyme, non-heme iron center, post-translational modification of cysteine residues, hydratase |
| Biological source | Rhodococcus erythropolis More |
| Total number of polymer chains | 4 |
| Total formula weight | 93663.27 |
| Authors | Nagashima, S.,Nakasako, M.,Dohmae, N.,Tsujimura, M.,Takio, K.,Odaka, M.,Yohda, M.,Kamiya, N.,Endo, I. (deposition date: 1997-12-24, release date: 1999-01-27, Last modification date: 2022-12-21) |
| Primary citation | Nagashima, S.,Nakasako, M.,Dohmae, N.,Tsujimura, M.,Takio, K.,Odaka, M.,Yohda, M.,Kamiya, N.,Endo, I. Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. Nat.Struct.Biol., 5:347-351, 1998 Cited by PubMed Abstract: The iron-containing nitrile hydratase (NHase) is a photoreactive enzyme that is inactivated in the dark because of persistent association with NO and activated by photo-dissociation of NO. The crystal structure at 1.7 A resolution and mass spectrometry revealed the structure of the non-heme iron catalytic center in the nitrosylated state. Two Cys residues coordinated to the iron were post-translationally modified to Cys-sulfenic and -sulfinic acids. Together with another oxygen atom of the Ser ligand, these modifications induced a claw setting of oxygen atoms capturing an NO molecule. This unprecedented structure is likely to enable the photo-regulation of NHase and will provide an excellent model for designing photo-controllable chelate complexes and, ultimately, proteins. PubMed: 9586994DOI: 10.1038/nsb0598-347 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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