Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin.

@article{Kamitani2010CharacterizationOT,
  title={Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin.},
  author={Shigeki Kamitani and Kengo Kitadokoro and Masayuki Miyazawa and Hirono Toshima and Aya Fukui and Hiroyuki Abe and Masami Miyake and Yasuhiko Horiguchi},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 33},
  pages={25467-75}
}
Pasteurella multocida toxin (PMT) is a virulence factor responsible for the pathogenesis of some forms of pasteurellosis. The toxin activates G(q)- and G(12/13)-dependent pathways through the deamidation of a glutamine residue in the alpha-subunit of heterotrimeric GTPases. We recently reported the crystal structure of the C terminus (residues 575-1285) of PMT (C-PMT), which is composed of three domains (C1, C2, and C3), and that the C1 domain is involved in the localization of C-PMT to the… CONTINUE READING

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