Amit Kumar and Mahejibin Khan Pages 281 - 288 ( 8 )
Under the environmental stress condition, protein folding or refolding has become an important issue for the survival of any microorganism. In majority of bacteria, such as Escherichia coli, temperature downshift leads to a transient arrest of cell growth, which results in inhibition of general protein synthesis. However, syntheses of a number of proteins, called cold-shock proteins are induced under these conditions. These proteins minimize secondary structure folding and acts as DNA or RNA chaperons. In the present study, to understand the mechanism of CSPs and to identify the key residues involved in nucleic acid binding, we generated homology model of cold shock protein homologs from CspB to CspI of Escherichia coli using Modeler 9v1. The modeled homologs were docked with potential ligand and protein-ligand interactions were studied using program, GLIDE. Docking results revealed that several basic and aromatic amino acid residues are conserved on the ligand binding surface of CSP homolog and aromatic residues that are essentially required for nucleic acid binding, also play important role in protein stability and protein folding inhibition.
Homology modeling, Molecular docking, Cold shock protein, GLIDE, Escherichia coli.
Central Food Technological Research Institute Resource Centre, Lucknow, UP 226018, India.