ISSN: 2576-7771
Authors: Joshi K and Laxman S Meena*
Tuberculosis (TB) is the major cause of mortality across the world. About one-third of world population is affected by this fatal disease. Mycobacterium tuberculosis H37Rv (M. tuberculosis) which is a gram- positive bacterium is responsible for the cause of TB.M. tuberculosis is spreading its roots worldwide with the help of various survival mechanisms and making its cure more difficult. In the present study, we have made use of various in-silico tools to predict the properties of Rv1651c which is a member of the PE_PGRS protein family. This manuscript reveals some important aspects of Rv1651c as its function is still unknown. The major part of this study includes protein sequence retrieval, multiple sequence alignment, protein-protein interaction study, epitope prediction, localization, function prediction, structure prediction and its validation, ligand binding prediction and mutational analysis. This protein shows the presence of GTP-binding motifs such as DXXG and GXXXXGK. These motifs can be targeted to mutate the protein and thereby, decrease its stability. This protein also shows similarity with enzyme ribose-5-phosphate isomerase, which performs the function of interconversion of ribose-5-phosphate and ribulose-5-phosphate. This similarity proves to be of great importance as this protein has ribulose-5-phosphate as one of its predicted ligands. All these in-silico generated results of Rv1651c give a hint of it being involved in carbohydrate metabolism. Carbohydrate metabolism is an important process required for the production of energy molecules. Thus, this protein might be targeted to block the carbohydrate metabolism pathway. These prediction-based studies using computational approach might prove to be a successful step towards developing drugs against TB.
Keywords: GTP Binding Protein; Ligand Binding; Mutational Analysis; Mycobacterium tuberculosis H37rv; Pe Pgrs Family; Ribose-5-Phosphate Isomerase
