Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress

Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification, The enzymes protect the cells against toxicants by conjugating them to glutathione, Recently, a novel subgroup of alpha-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress, Here, me report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup, The structure was solved by molecular replacement and refined to 2.9 Angstrom resolution, It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site. (C) 1998 Federation of European Biochemical Societies