Molecular Dynamics Study of Glutathione S-Transferase: Structure and Binding Character of Glutathione

Abstract

Molecular dynamics simulations of the glutathione S-transferase (GST) dimer in the absence or the presence of glutathione were carried out in order to investigate the binding effects of glutathione on the dynamical structure and thermal stability of the GST dimer in water. Enhanced local fluctuations in the GST dimer backbone were observed in the absence of glutathione. The hydrogen bonds formed between glutathione and the GST dimer were changed in the absence of glutathione, and these hydrogen bonds mediate the binding between the subunits of the GST dimer. The free energy analysis showed that the hydrogen bonds between glutathione and the GST dimer largely contribute to the binding energy of glutathione and the thermal stability of the glutathione-GST dimer.