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

FEBS Letters

Arkema, Anita¹  Zimniak, Piotr²  Dijkstra, Bauke W¹  Hoier, Helga¹  Kalk, Kor H¹  Krengel, Ute¹  Schröter, Klaus-Hasso¹ 

[1] Laboratory of Biophysical Chemistry and BIOSON Research Institute, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands;Departments of Medicine, and Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA

关键词: Crystal structure;    Glutathione;    Glutathione S-transferase;    Lipid peroxidation;    Oxidative stress;    GST;    glutathione S-transferase;    MPD;    2-methyl-2;    4-pentanediol;    r.s.c.c.;    real space correlation coefficient;    r.m.s.d.;    root mean square difference;   

DOI  :  10.1016/S0014-5793(98)00026-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown