Identification, characterization, and crystal structure of the Omega class glutathione transferases.
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.
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PG
Molecular Genetics Group and Human Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Coggan
M
M
Chelvanayagam
G
G
Easteal
S
S
Jermiin
L S
LS
Schulte
G K
GK
Danley
D E
DE
Hoth
L R
LR
Griffor
M C
MC
Kamath
A V
AV
Rosner
M H
MH
Chrunyk
B A
BA
Perregaux
D E
DE
Gabel
C A
CA
Geoghegan
K F
KF
Pandit
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017173:Caenorhabditis elegans / Q000201:enzymology; D018360:Crystallography, X-Ray; D005260:Female; D005982:Glutathione Transferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008322:Mammals; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016324:Sequence Tagged Sites; D013379:Substrate Specificity; D014158:Transcription, Genetic
D007527:Isoenzymes; D005982:Glutathione Transferase