1guk | pdb_00001guk
CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4
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| 1guk, resolution 2.9Å | |||||||||||||
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| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1GUK is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
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