Crystal structure of Mycobacterium tuberculosis VapC20 toxin and its interactions with cognate antitoxin, VapB20, suggest a model for toxin-antitoxin assembly.

@article{Deep2017CrystalSO,
  title={Crystal structure of Mycobacterium tuberculosis VapC20 toxin and its interactions with cognate antitoxin, VapB20, suggest a model for toxin-antitoxin assembly.},
  author={Amar Deep and Soni Kaundal and Sakshi Agarwal and Ramandeep Singh and Krishan Gopal Thakur},
  journal={The FEBS journal},
  year={2017},
  volume={284 23},
  pages={4066-4082}
}
VapBCs, virulence-associated proteins, are the most abundant type II toxin-antitoxin (TA) systems in prokaryotes. Under normal conditions, toxin and antitoxin interact to form a heterooctameric complex, which upon binding to operator sites, inhibits their own expression. Under stress conditions, the VapB antitoxin is degraded by cellular proteases to… CONTINUE READING