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1ire
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Nitrile hydratase, with EC number 4.2.1.84 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
Overview
The crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two cysteine residues (alphaCys(111) and alphaCys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (betaTrp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase.
About this Structure
1IRE is a Protein complex structure of sequences from Pseudonocardia thermophila. Full crystallographic information is available from OCA.
Reference
Crystal structure of cobalt-containing nitrile hydratase., Miyanaga A, Fushinobu S, Ito K, Wakagi T, Biochem Biophys Res Commun. 2001 Nov 16;288(5):1169-74. PMID:11700034
Page seeded by OCA on Sun Mar 30 21:23:35 2008
