Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient.

@article{Krantz2006ProteinTT,
  title={Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient.},
  author={Bryan A. Krantz and Alan Finkelstein and Robert J. Collier},
  journal={Journal of molecular biology},
  year={2006},
  volume={355 5},
  pages={
          968-79
        }
}
  • Bryan A. Krantz, Alan Finkelstein, Robert J. Collier
  • Published in Journal of molecular biology 2006
  • Chemistry, Medicine
  • Protective antigen (PA) from anthrax toxin assembles into a homoheptamer on cell surfaces and forms complexes with the enzymatic components: lethal factor (LF) and edema factor (EF). Endocytic vesicles containing these complexes are acidified, causing the heptamer to transform into a transmembrane pore that chaperones the passage of unfolded LF and EF into the cytosol. We show in planar lipid bilayers that a physiologically relevant proton gradient (DeltapH, where the endosome is acidified… CONTINUE READING

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