Title

Authors

Gagan Chhabra¹, Aparna Dixit², Lalit C. Garg¹*

Affiliation

¹Gene Regulation Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi- 110067, India; ²Gene Regulation Laboratory, School of Biotechnology, Jawaharlal Nehru University, New Delhi- 110067, India 

Email

lalit@nii.res.in; *Corresponding author

Phone

+91 11 26703652

Fax

+91 11 26742125

Article Type

Hypothesis

Date

Received March 03, 2011; Accepted March 16, 2011; Published March 26, 2011

The alpha subunit of Mycobacterial DNA polymerase III holo enzyme catalyzes the polymerization of both DNA strands. The present investigation reports three dimensional (3-D) structure model of DNA polymerase III a subunit of Mycobacterium tuberculosis H37Rv (MtbDnaE1) generated using homology modeling with the backbone structure of DNA polymerase III a of Thermus aquaticus as a template. The model was evaluated at various structure verification servers, which assess the stereo chemical parameters of the residues in the model, as well as structural and functional domains. Comparative analysis of MtbDnaE1 structure reveals the structure of its catalytic domain to be unrelated to that of the human. Successful docking of known inhibitor of bacterial DNA polymerases, 251D onto the modeled MtbDnaE1 was also performed. Therefore, the structure model of MtbDnaE1, a potential anti-mycobacterial target, opens a new avenue for structure-based drug designing against the pathogen.  

Keywords

Mycobacterium tuberculosis; DNA polymerase III a subunit; homology modeling; drug designing

Citation

Chhabra et al. Bioinformation 6(2): 69-73 (2011)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.