Human glutathione synthetase (hGS) has been shown by our laboratory to be an obligate homodimer that is negatively cooperative for the binding of gamma-glutamylcysteine. Through a combination of experiment (site directed mutatgenesis, enzyme kinetics, etc.) and modeling (docking, molecular dynamics, etc.) two novel structures within hGS have been identified, the so-called H- and E-loops that mediate communication between the substrate binding site and the dimer interface. This presentation discusses our latest research to delineate the complete allosteric pathway of hGS and its implications for understanding the biochemistry of glutathione, protein allostery and protein:protein interaction.

H-loop and E-loop of human glutathione synthetase

249th National Meeting (2015)

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