2ahj
From Proteopedia
|
NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE
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 [[1]], with EC number [4.2.1.84]. 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
Page seeded by OCA on Mon Oct 29 19:26:40 2007
Categories: 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
