1GUK

CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4

Summary for 1GUK

• Entry DOI: 10.2210/pdb1guk/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE A4-4 (1 entity in total)
• Functional Keywords: glutathione s-transferase, gst, oxidative stress, transferase
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: P24472
• Total number of polymer chains: 2
• Total formula weight: 51215.84

Authors

Krengel, U.,Schroter, K.H.,Hoier, H.,Dijkstra, B.W. (deposition date: 1997-12-11, release date: 1998-04-08, Last modification date: 2024-05-22)

Primary citation

Krengel, U.,Schroter, K.H.,Hoier, H.,Arkema, A.,Kalk, K.H.,Zimniak, P.,Dijkstra, B.W.
Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress.
FEBS Lett., 422:285-290, 1998

PubMed Abstract: 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.

PubMed: 9498801
DOI: 10.1016/S0014-5793(98)00026-X

Experimental method

X-RAY DIFFRACTION (2.9 Å)