Large-scale structural changes accompany binding of lethal factor to anthrax protective antigen: a cryo-electron microscopic study.

@article{Ren2004LargescaleSC,
  title={Large-scale structural changes accompany binding of lethal factor to anthrax protective antigen: a cryo-electron microscopic study.},
  author={Gang Ren and Joel Ivan Munoz Quispe and Stephen H Leppla and Alok K Mitra},
  journal={Structure},
  year={2004},
  volume={12 11},
  pages={2059-66}
}
Anthrax toxin (AT), secreted by Bacillus anthracis, is a three-protein cocktail of lethal factor (LF, 90 kDa), edema factor (EF, 89 kDa), and the protective antigen (PA, 83 kDa). Steps in anthrax toxicity involve (1) binding of ligand (EF/LF) to a heptamer of PA63 (PA63h) generated after N-terminal proteolytic cleavage of PA and, (2) following endocytosis of the complex, translocation of the ligand into the cytosol by an as yet unknown mechanism. The PA63h.LF complex was directly visualized… CONTINUE READING
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