The mechanism of pore formation by bacterial toxins.

@article{Tilley2006TheMO,
  title={The mechanism of pore formation by bacterial toxins.},
  author={Sarah J. Tilley and Helen R Saibil},
  journal={Current opinion in structural biology},
  year={2006},
  volume={16 2},
  pages={230-6}
}
A remarkable group of proteins challenge the notions that protein sequence determines a unique three-dimensional structure, and that membrane and soluble proteins are very distinct. The pore-forming toxins typically transform from soluble, monomeric proteins to oligomers that form transmembrane channels. Recent structural studies provide ideas about how these changes take place. The recently solved structures of the beta-pore-forming toxins LukS, epsilon-toxin and intermedilysin confirm that… CONTINUE READING

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