A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.

@article{Krantz2005APC,
  title={A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore.},
  author={Bryan A Krantz and Roman A Melnyk and Sen Zhang and Stephen J. Juris and D Borden Lacy and Zhengyan Wu and Alan Finkelstein and Robert J. Collier},
  journal={Science},
  year={2005},
  volume={309 5735},
  pages={777-81}
}
The protective antigen component of anthrax toxin forms a homoheptameric pore in the endosomal membrane, creating a narrow passageway for the enzymatic components of the toxin to enter the cytosol. We found that, during conversion of the heptameric precursor to the pore, the seven phenylalanine-427 residues converged within the lumen, generating a radially symmetric heptad of solvent-exposed aromatic rings. This "phi-clamp" structure was required for protein translocation and comprised the… CONTINUE READING

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