Identification, characterization, and crystal structure of the omega class glutathione transferases

被引:584
作者
Board, PG
Coggan, M
Chelvanayagam, G
Easteal, S
Jermiin, LS
Schulte, GK
Danley, DE
Hoth, LR
Griffor, MC
Kamath, AV
Rosner, MH
Chrunyk, BA
Perregaux, DE
Gabel, CA
Geoghegan, KF
Pandit, J
机构
[1] Australian Natl Univ, John Curtin Sch Med Res, Mol Genet Grp, Canberra, ACT 2601, Australia
[2] Australian Natl Univ, John Curtin Sch Med Res, Human Genet Grp, Canberra, ACT 2601, Australia
[3] Univ Sydney, Australian Genom Informat Ctr, Sydney, NSW 2006, Australia
[4] Pfizer Global Res & Dev, Groton, CT 06340 USA
关键词
D O I
10.1074/jbc.M001706200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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-Angstrom resolution and has a characteristic GST fold (Protein Data Bank entry code leem). 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,
引用
收藏
页码:24798 / 24806
页数:9
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