Structure Function Analysis of Proteins in M. tuberculosis

Exploiting the state-of-art technology for increasing the knowledge base on micro organisms, scientists at NCCS are studying the structure and functional correlation of proteins derived from Mycobacterium tuberculosis. Using crystallography and in-silico methods, they are analyzing the heat shock responses mediated by proteins such as GroEL chaperonin, oxidative stress induced redox reactions and enzymatic reaction mediated electron transport mechanisms in the cell.


Figure 1: Crystal structure of NrdH from M. tuberculosis, refined to a crystallographic R factor of 14.02% (Rfree = 15.53%) at 0.87 Å resolution.

Potential application of this research is for developing better therapeutics for tuberculosis.


  1. GroEL2 OF tuberculosis Reveals The Importance Of Structural Pliability In Chaperonin Function, J Bacteriol. 2015 Nov 9. pii: JB.00844-15 (Article).
  2. The Crystal Structure of Mycobacterium tuberculosisNrdH at 0.87 Å Suggests a Possible Mode of Its Activity, Biochemistry 2013, 52, 4056−4065 (Article).
  3. Identification of the INO1 Gene of Mycobacterium tuberculosis H37Rv Reveals a Novel Class of Inositol-1-phosphate Synthase Enzyme, J. Mol. Biol. (1999) 291, 531-536 (Article).

Technology Readiness: TRL B

Technology Status: Proprietary Know-how

Technology Availability: Know-how available for co-development.