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2ahj
From Proteopedia
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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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:28 2008'' |
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 , , , and as ligands. Active as Nitrile hydratase, with EC number 4.2.1.84 Known structural/functional Sites: , and . 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 Thu Feb 21 16:27:28 2008
Categories: 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
