X-ray Crystal Structures of Cytosolic Glutathione S-transferases. Implications for Protein Architecture, Substrate Recognition and Catalytic Function

Eur J Biochem. 1994 Mar 15;220(3):645-61. doi: 10.1111/j.1432-1033.1994.tb18666.x.

Abstract

Crystal structures of cytosolic glutathione S-transferases (EC 2.5.1.18), complexed with glutathione or its analogues, are reviewed. The atomic models define protein architectural relationships between the different gene classes in the superfamily, and reveal the molecular basis for substrate binding at the two adjacent subsites of the active site. Considerable progress has been made in understanding the mechanism whereby the thiol group of glutathione is destabilized (lowering its pKa) at the active site, a rate-enhancement strategy shared by the soluble glutathione S-transferases.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalysis
  • Crystallography, X-Ray
  • Cytosol / enzymology
  • Glutathione / chemistry
  • Glutathione Transferase / chemistry
  • Glutathione Transferase / ultrastructure*
  • Ligands
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Substrate Specificity
  • Swine

Substances

  • Ligands
  • Glutathione Transferase
  • Glutathione