Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress.
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.
Krengel
U
U
BIOSON Research Institute, Department of Chemistry, University of Groningen, The Netherlands.
Schröter
K H
KH
Hoier
H
H
Arkema
A
A
Kalk
K H
KH
Zimniak
P
P
Dijkstra
B W
BW
D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D005978:Glutathione / Q000378:metabolism; D005982:Glutathione Transferase / Q000737:chemistry* / Q000378:metabolism; D007526:Isoelectric Point; D051379:Mice; D008958:Models, Molecular; D018384:Oxidative Stress; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D005982:Glutathione Transferase; D005978:Glutathione