2ahj: Difference between revisions
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==Overview== | ==Overview== | ||
The iron-containing nitrile hydratase (NHase) is a photoreactive enzyme | 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== | ==About this Structure== | ||
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[[Category: post-translational modification of cysteine residues]] | [[Category: post-translational modification of cysteine residues]] | ||
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Revision as of 14:27, 21 February 2008
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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 Nitrile hydratase, with EC number 4.2.1.84 Known structural/functional 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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
