X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
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.
Dirr
H
H
Department of Biochemistry, University of the Witwatersrand, Johannesburg, South Africa.
Reinemer
P
P
Huber
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D003600:Cytosol / Q000201:enzymology; D005978:Glutathione / Q000737:chemistry; D005982:Glutathione Transferase / Q000737:chemistry / Q000648:ultrastructure*; D008024:Ligands; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013552:Swine
D008024:Ligands; D005982:Glutathione Transferase; D005978:Glutathione