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

Ute Krengel, Klaus-Hasso Schröter, Helga Hoier, Anita Arkema, Kor H. Kalk, Piotr Zimniak, Bauke W. Dijkstra

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    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 α-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 Å resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site.
    Original languageEnglish
    Pages (from-to)285-290
    Number of pages6
    JournalFEBS Letters
    Publication statusPublished - 1998


    • Oxidative stress
    • Lipid peroxidation
    • Glutathione S-transferase
    • Glutathione
    • Crystal structure

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