Molecular Modeling and Insilico Structural analysis of Mycobacterium Tuberculosis Mycosin 1

Author Name(s): *J. Harini
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The Mycosins are subtilin like serine proteases present in Mycobacterium Tuberculosis. They have been reported to play a prominent role in Lysin degradation and Biotin metabolism. MycP-1 protein is one of the major proteins expressed in the patients infected with Mycobacterium Tuberculosis. The key metabolic process involved in Bacilli growth and survival is Biotin synthesis. Thus use of anti tubercular agents against the proteins involved in Biotin synthesis like Mycosins can combat the pathogenic effect caused due to Tuberculosis. The current work aims at constructing the protein model of MycP1 protein and interaction with its corresponding substrates. The Homology studies between various mycosin proteins and phylogenic analysis was carried out to determine the evolutionary strength among the proteins. To characterize the physicochemical and stereo chemical properties of MycP1 Functional and Structural analysis was performed. As the 3D structure determination of MycP1 was not reported. Using the Homology Modeling Approach, A protein model has been built. The model was developed using the Ab Initio Structure Prediction Method and further validated using Stereochemical analysis. Docking of substrates with Mtb-MycP1 has been performed to investigate the binding properties and energies of potent substrate of Mtb-MycP1 so as to propose effective and selective Mtb drugs for experimental validation.


Mycosins, Mycobacterium tuberculosis, Ab initio structure prediction


Mycobacterium tuberculosis (M.tb) is the causative agent of tuberculosis (TB) and a successful pathogen that overcomes the numerous challenges presented by the immune system of the host. TB remains one of the world’s greatest causes of mortality and morbidity, with approximately 8 million new infections and 2 million deaths per year [1] More adults die due to TB every year than AIDS and Malaria together [2]. The Mtb genome revealed the presence of a large number of putative protease genes, some encoding potential secreted proteases [3]. This includes a family of five subtilisin –like serine proteases, the mycosins [4], which share a high
Degree of similarity and are constitutively expressed in M. tuberculosis H37Rv [5]. The gene was found to be situated at 3700 bp (four ORF’s) from the RD1 deletion region, which has attracted considerable attention recently because of possibly being a locus for potential diagnostic proteins. An observation of importance in homology modeling is that for a set of proteins that are hypothesized to be homologous, their three-dimensional structures are conserved to a greater extent when compared to their primary structures. This observation has been used to generate models of proteins from homologues with very low sequence similarities. Thus, in homology modeling, we are attempting to construct model of MycP1 from homologous proteins and analyzing the functional properties by performing Dockings.


3D Protein Structure of MycP1 was modeled and is validated using ramachandran plot. Structural analysis was performed and the functionality of the protein was analyzed by docking with the substrates. The results showed the best docking confirmations with the lowest binding energy and the greatest number of Conformations per cluster.

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