New mutations in the mycobacterial ATP synthase: new insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure.

@article{Segala2012NewMI,
  title={New mutations in the mycobacterial ATP synthase: new insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure.},
  author={Elena Segala and Wladimir Sougakoff and Aurelie Nevejans-Chauffour and Vincent Jarlier and St{\'e}phanie Petrella},
  journal={Antimicrobial agents and chemotherapy},
  year={2012},
  volume={56 5},
  pages={
          2326-34
        }
}
TMC207 is a new antituberculous drug belonging to the diarylquinoline class which very efficiently inhibits the ATP synthase of mycobacteria such as Mycobacterium tuberculosis, one of the most important pathogens in the world. In order to map the amino acid residues involved in the binding of the drug, we have selected in vitro TMC207-resistant mutants from M. tuberculosis and diverse atypical mycobacteria. Six distinct mutations, Asp28 → Gly, Asp28 → Ala, Leu59 → Val, Glu61 → Asp, Ala63 → Pro… CONTINUE READING

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