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

J Biol Chem. 2000 Aug 11;275(32):24798-806. doi: 10.1074/jbc.M001706200.

P G Board ¹, M Coggan, G Chelvanayagam, S Easteal, L S Jermiin, G K Schulte, D E Danley, L R Hoth, M C Griffor, A V Kamath, M H Rosner, B A Chrunyk, D E Perregaux, C A Gabel, K F Geoghegan, J Pandit

Affiliations

Affiliation

1 Molecular Genetics Group and Human Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory 2601, Australia.

PMID: 10783391 DOI: 10.1074/jbc.M001706200

Abstract

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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