Crystal structure of a theta-class glutathione transferase

M. C J Wilce, P. G. Board, S. C. Feil, M. W. Parker

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Abstract

Glutathione S-transferases (GSTs) are a family of enzymes involved in the cellular detoxification of xenotoxins. Cytosolic GSTs have been grouped into four evolutionary classes for which there are representative crystal structures of three of them. Here we report the first crystal structure of a theta-class GST. So far, all available GST crystal structures suggest that a strictly conserved tyrosine near the N-terminus plays a critical role in the reaction mechanism and such a role has been convincingly demonstrated by site-directed mutagenesis. Surprisingly, the equivalent residue in the theta-class structure is not in the active site, but its role appears to have been replaced by either a nearby serine or by another tyrosine residue located in the C-terminal domain of the enzyme.

Original languageEnglish
Pages (from-to)2133-2143
Number of pages11
JournalThe EMBO Journal
Volume14
Issue number10
Publication statusPublished - 1 Jan 1995
Externally publishedYes

Keywords

  • Detoxification
  • Evolution
  • Glutathione S-transferase
  • Structural similarity
  • X-ray crystallography

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