Crystal structure of cobalt-containing nitrile hydratase.
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.
Miyanaga
A
A
Department of Biotechnology, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Fushinobu
S
S
Ito
K
K
Wakagi
T
T
D000192:Actinomycetales / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D003035:Cobalt / Q000737:chemistry*; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D006836:Hydro-Lyases / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry; D008956:Models, Chemical; D018377:Neurotransmitter Agents; D011499:Protein Processing, Post-Translational; D013434:Sulfenic Acids / Q000378:metabolism
D001426:Bacterial Proteins; D018377:Neurotransmitter Agents; D013434:Sulfenic Acids; D003035:Cobalt; D007501:Iron; D006836:Hydro-Lyases; C048831:nitrile hydratase; C100870:cysteinesulfenic acid; D003545:Cysteine; C013461:cysteine sulfinic acid