Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly.

@article{Das2014CrystalSO,
  title={Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly.},
  author={Uddipan Das and Vivian Pogenberg and Udaya Kumar Tiruttani Subhramanyam and Matthias Wilmanns and Samudrala Gourinath and Alagiri Srinivasan},
  journal={Journal of structural biology},
  year={2014},
  volume={188 3},
  pages={249-58}
}
Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins. Here we present the crystal structure of the VapBC-15 toxin-antitoxin complex from Mycobacterium tuberculosis determined to 2.1Å resolution. The VapB-15 and VapC-15 components assemble into one… CONTINUE READING

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