Structure/function studies of pi and theta class glutathione transferases

A. J. Oakley, J. Rossjohn, W. J. McKinstry, J. Flanagan, P. G. Board, M. Lo Bello, G. Ricci, M. W. Parker

Research output: Contribution to journalArticleResearchpeer-review


Here we review our recent crystallographic studies of glutathione S-transferases (GSTs) with a particular emphasis on human class pi and theta enzymes. We first determined the structure of human pi class GST in 1992. These studies have been extended to the structure determination of numerous enzyme complexes, which have revealed the intricate details of how substrates and inhibitors are bound to the enzyme and further details of the reaction mechanism. We have recently determined the first human theta class GST. This structure revealed a number of surprises including the existence of a sulfate binding pocket and a buried active site.

Original languageEnglish
Pages (from-to)231-238
Number of pages8
JournalClinical Chemistry and Enzymology Communications
Issue number4-6
Publication statusPublished - 1 Dec 1999
Externally publishedYes


  • Enzyme-inhibitor complexes
  • Pi class GSTs
  • Sulfatase
  • Theta class GSTs
  • X-ray crystallography

Cite this