Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases*

By P. Board, M. Coggan, G. Chelvanayagam, Simon Easteal, Lars S. Jermiin, G. Schulte, D. Danley, L. R. Hoth, M. Griffor, A. Kamath and 6 more. Journal of Biological Chemistry, 2000

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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 andCaenorhabditis 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-Å resolution and has a characteristic GST fold (Protein Data Bank entry code 1eem). 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.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3a786f624c2391e081e483182b5ca4bd057044c4

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