Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC.

@article{Mavrici2014MycobacteriumTF,
  title={Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC.},
  author={Daniela Mavrici and Mohlopheni J Marakalala and James M. Holton and Daniil M Prigozhin and Christine L Gee and Yanjia J. Zhang and Eric J. Rubin and Tom Alber},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 22},
  pages={8037-42}
}
Bacterial growth and cell division are coordinated with hydrolysis of the peptidoglycan (PG) layer of the cell wall, but the mechanisms of regulation of extracellular PG hydrolases are not well understood. Here we report the biochemical, structural, and genetic analysis of the Mycobacterium tuberculosis homolog of the transmembrane PG-hydrolase regulator, FtsX. The purified FtsX extracellular domain binds the PG peptidase Rv2190c/RipC N-terminal segment, causing a conformational change that… CONTINUE READING
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