Insilico analysis and molecular docking of resuscitation promoting factor B (RpfB) protein of Mycobacterium tuberculosis

Invulnerability of Mycobacterium tuberculosis to various drugs and its persistency has stood as a hurdle in the race againsteradication of the pathogenecity of the bacteria. Identification of novel antituberculosis compounds is highly demanding as theavailable drugs are resistant. The ability of the bacteria to surpass the body''s defenses and adapt itself to survive for diseasereactivation is contributed by secreted proteins called resuscitating promoting factors (Rpfs). These factors aid in virulence andresuscitation from dormancy of the bacteria. Sequence analysis of RpfB was performed and compounds were first screened fortoxicity and high-throughput virtual screening eliminating the toxic compounds. To understand the mechanism of ligand bindingand interaction, molecular docking was performed for the compounds passing through the filter resulting with better dockingstudies predicting the possible binding mode of the inhibitors to the protein. Of all the active residues the binding conformationshows that residues Arg194, Arg196, Glu242, and Asn244 of the RpfB protein play vital role in the enzyme activity and interactswith the ligands. Promising compounds have been identified in the current study, thus holding promise for design of antituberculosisdrugs.