1IRE

Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila

Summary for 1IRE

• Entry DOI: 10.2210/pdb1ire/pdb
• Descriptor: Nitrile Hydratase, COBALT (II) ION, ... (4 entities in total)
• Functional Keywords: cysteine-sulfinic acid, cysteine-sulfenic acid, post-translational modification, non-corrin cobalt, nitrile, hydration, lyase
• Biological source: Pseudonocardia thermophila; More
• Total number of polymer chains: 2
• Total formula weight: 49448.67

Authors

Miyanaga, A.,Fushinobu, S.,Ito, K.,Wakagi, T. (deposition date: 2001-10-01, release date: 2002-10-01, Last modification date: 2024-11-20)

Primary citation

Miyanaga, A.,Fushinobu, S.,Ito, K.,Wakagi, T.
Crystal structure of cobalt-containing nitrile hydratase.
Biochem.Biophys.Res.Commun., 288:1169-1174, 2001

PubMed Abstract: 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.

PubMed: 11700034
DOI: 10.1006/bbrc.2001.5897

Experimental method

X-RAY DIFFRACTION (1.8 Å)