Crystal structures of cytosolic glutathione S-transferases (EC 184.108.40.206), 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.
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hGSTA1-1, rGSTM1-1 etc., acronyms for the glutathione S-transferases (GST), the prefix indicating the species (p, porcine
guinea pig) while P, A, and M indicate gene class pi, alpha and mu, respectively; 1-1 indicates a dimer of two type-1 subunits
P2 etc. and G1, G2 etc., designate peptide functional groups in glutathione and the corresponding G-site ligands of the glutathione S-transferases, respectively
hydrophobic electrophile-binding site
Glutathione S-transferase (EC 220.127.116.11)