Publication Abstract from PubMed
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, we 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 A resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site.
Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress.,Krengel U, Schroter KH, Hoier H, Arkema A, Kalk KH, Zimniak P, Dijkstra BW FEBS Lett. 1998 Feb 6;422(3):285-90. PMID:9498801[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
