<I>In Silico</I> Comparative Modeling of clpP2 Protein from (<I>Mycobacterium tuberculosis</I> H37Rv)

Abstract

Tuberculosis remains one of the major threats to human health, Mycobacterium tuberculosis , a gram-positive bacterium kills two or three million people per year.ATPdependent Clp protease (ClpP) is a core unit of a major bacterial protease complex. The Mycobacterium tuberculosis (MTB) genome contains two genes coding for putative ClpPs, ClpP1 and ClpP2 respectively, that are likely to play a role in the virulence of the bacterium. ClpP2 employing as a new attractive drug target for that isolates ClpP2 involved in bacteria growth and oxidative stress tolerance. In the present study a complete structural analysis and 3-D modelling of clpP2 protein of Mycobacterium tuberculosis , was carried out. The 214 amino acid sequence of the clpP2 protein was retrieved from NCBI database. Based on the PDB Blast report, PDB file of ClpP from E. coli was used as template for three dimensional structure of the clpP2 protein, was predicted by using the software MODELLER 9v9.The template protein exposed 49% sequence identity with clpp2 protein. The computed model’s energy was minimized and validated using PROCHECK to obtain a stable model structure. Ramachandran plot showed that, fur protein have 94.7% fully allowed region, 5.3% additionally allowed region, 0.0% generously allowed region and 0.0% disallowed region and later then is submitted in Protein Model Database (PMDB-ID: PM0077929) . The model might be elucidated the use in additional functional characterization of this protein.