2ahj | pdb_00002ahj
NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE
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Overview
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.
About this Structure
2AHJ is a [Protein complex] structure of sequences from [Rhodococcus erythropolis] with FE, ZN, SO4, NO and DIO as [ligands]. Active as [Nitrile hydratase], with EC number [4.2.1.84]. Structure known Active Sites: 1, CTA and CTB. Full crystallographic information is available from [OCA].
Reference
Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms., Nagashima S, Nakasako M, Dohmae N, Tsujimura M, Takio K, Odaka M, Yohda M, Kamiya N, Endo I, Nat Struct Biol. 1998 May;5(5):347-51. PMID:9586994
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- Nitrile hydratase
- Protein complex
- Rhodococcus erythropolis
- Dohmae, N.
- Endo, I.
- Kamiya, N.
- Nagashima, S.
- Nakasako, M.
- Odaka, M.
- Takio, K.
- Tsujimura, M.
- Yohda, M.
- DIO
- FE
- NO
- SO4
- ZN
- Hydratase
- Lyase
- Nitric oxide binding enzyme
- Non-heme iron center
- Photoreactive enzyme
- Post-translational modification of cysteine residues
