Electrostatic properties of Escherichia coli wild-type and mutant arginine repressor C-terminal domain (ArgRc) protein-ligand complexes: Insights into molecular interaction and function
Rowyna Kueh1, Abd Rahman Noorsaadah1*, and Merican Amir Faisal2
1Chemistry Department, 2Institute of Biological Sciences, Faculty of Science,University of Malaya, 50603 Kuala Lumpur, Malaysia
*Author for Correspondence.
Chemistry Department,
Faculty of Science,
University of Malaya, 50603
Kuala Lumpur, Malaysia.
Tel: (603)79674254; Fax: (603)79674193;
Email: noorsaadah@um.edu.my
Abstract.
Electrostatic potential calculations were performed in order to understand the effect of long-range electrostatic interactions of L-arginine, L-canavanine and L-citrulline in binding to the Escherichia coli arginine repressor C-terminal domain (ArgRc. The three ligands were also subjected to the same studies while bound to a mutant protein, ArgRc(D128N). The results showed significant changes in the electrostatic potential of ArgRc and ArgRc(D128N) due to L-arginine binding while no significant changes were observed for ArgRc and ArgRc(D128N) bound to either L-canavanine or L-citrulline. The study also revealed changes in the electrostatic potential of ArgRc(D128N) that may explain the ability of ArgRc(D128N) to act as a superrepressor.
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