National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
Mycobacterium tuberculosis (Mtb), the causative agent of the disease tuberculosis, is an ancient pathogen and a major cause of death worldwide. Although various virulence factors of M. tb have been identified, its pathogenesis remains incompletely understood. TlyA is a virulence factor that is evolutionarily conserved in many gram-positive bacteria, but its full length structure and function in the pathogenesis of infection with Mtb has not been elucidated. In the present study, we cloned, expressed and purified N-terminal domain of tlyA, which play a crucial role in the binding of the co-substrate S-adenosyl-L-methionine. We characterized the protein by SDS-PAGE and Circular Dichroism. TlyA model generated using tlyA crystal structure, clearly indicates E59 separates between N-terminal domain (NTD) and C-terminal domain (CTD).
Mycobacterium tuberculosis, N-terminal domain, Circular dichroism, tlyA, Maltose binding protein
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