2ahj

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==Overview==
==Overview==
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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.
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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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''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


2ahj, resolution 1.7Å

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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

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