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International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
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National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2019)
[Effective from January 1, 2019]
For more details click here

ICV 2017: 100.00
Index Copernicus ICI Journals Master List 2017 - IJCMAS--ICV 2017: 100.00
For more details click here

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Original Research Articles

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 2017: 100.00
NAAS RATING 2018: 5.38

Int.J.Curr.Microbiol.App.Sci.2019.8(9): 2203-2212
DOI: https://doi.org/10.20546/ijcmas.2019.809.254


Mycobacterium tuberculosis tlyA E59Q is Stable Compared to the Native Protein
V. B. Shivaleela1, ShaikKalimulla Niazi2, P. Sharada1* and K. Giri Gowda3*
1Department of Biotechnology, Basaveshwara Engineering College, Bagalkot-587102, Karnataka, India
2Department of Biotechnology, Preparatory Health Sciences, Riyadh Elm University,
Riyadh, Saudi Arabia
3Sampoorna International Institute of Agri.Science & Horticulture Technology,
Mandya-571433, Karnataka, India
*Corresponding author
Abstract:

The causative agent of human tuberculosis disease, mycobacterium tuberculosis (Mtb), infects one-third of the world population. Mycobacterium tuberculosis tlyA is an important protein and the mutation can cause resistance to antibiotics. Understanding the structure-function of mycobacterium tuberculosis tlyA is essential for preventing antibiotic resistance. Structure of Mycobacterium tuberculosis CTD of tlyA structure was solved, whereas its biological functions are not fully understood. Here, we studied tlyA protein by mutational analysis and molecular modelling studies. Further, purified tlyA is found to be very stable compared to the native tlyA and retained its three dimensional structure. In the absence of full length tlyA structure, molecular model was generated by I-Tasser server using tlyA CTD crystal structure as a template. Generated model showed 90% of residues in the allowed region, 7% in additional allowed region and 3% residues in disallowed region. These results reveal Mtb-tlyA NTD is important for its structure and function and E59Q is a critical residue for retaining the N-terminus.


Keywords: tlyA, Mycobacterium tuberculosis, methyltransferase, antibiotic resistance, mutation.
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How to cite this article:

Shivaleela, V. B., ShaikKalimulla Niazi, P. Sharada and Giri Gowda, K. 2019. Mycobacterium tuberculosis tlyA E59Q is Stable Compared to the Native Protein.Int.J.Curr.Microbiol.App.Sci. 8(9): 2203-2212. doi: https://doi.org/10.20546/ijcmas.2019.809.254