2qdy

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{{STRUCTURE_2qdy| PDB=2qdy | SCENE= }}
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'''Crystal Structure of Fe-type NHase from Rhodococcus erythropolis AJ270'''
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===Crystal Structure of Fe-type NHase from Rhodococcus erythropolis AJ270===
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==Overview==
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The crystal structure of Fe-type nitrile hydratase from Rhodococcus erythropolis AJ270 was determined at 1.3A resolution. The two cysteine residues (alphaCys(112) and alphaCys(114)) equatorially coordinated to the ferric ion were post-translationally modified to cysteine sulfinic acids. A glutamine residue (alphaGln(90)) in the active center gave double conformations. Based on the interactions among the enzyme, substrate and water molecules, a new mechanism of biocatalysis of nitrile hydratase was proposed, in which the water molecule activated by the glutamine residue performed as the nucleophile to attack on the nitrile which was simultaneously interacted by another water molecule coordinated to the ferric ion.
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(as it appears on PubMed at http://www.pubmed.gov), where 17716629 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17716629}}
==About this Structure==
==About this Structure==
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[[Category: Nitrile hydratase]]
[[Category: Nitrile hydratase]]
[[Category: Post translation]]
[[Category: Post translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:31:58 2008''

Revision as of 18:32, 28 July 2008

Image:2qdy.png

Template:STRUCTURE 2qdy

Crystal Structure of Fe-type NHase from Rhodococcus erythropolis AJ270

Template:ABSTRACT PUBMED 17716629

About this Structure

2QDY is a Protein complex structure of sequences from Rhodococcus erythropolis. Full crystallographic information is available from OCA.

Reference

High resolution X-ray molecular structure of the nitrile hydratase from Rhodococcus erythropolis AJ270 reveals posttranslational oxidation of two cysteines into sulfinic acids and a novel biocatalytic nitrile hydration mechanism., Song L, Wang M, Shi J, Xue Z, Wang MX, Qian S, Biochem Biophys Res Commun. 2007 Oct 19;362(2):319-24. Epub 2007 Aug 14. PMID:17716629

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