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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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.[1]

References

  1. Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress. Krengel, U., Schröter, K.H., Hoier, H., Arkema, A., Kalk, K.H., Zimniak, P., Dijkstra, B.W. FEBS Lett. (1998) [Pubmed]
 
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