Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.

@article{Heuck2000MechanismOM,
  title={Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.},
  author={Alejandro P Heuck and Eileen M. Hotze and Rodney K. Tweten and Arthur E. Johnson},
  journal={Molecular cell},
  year={2000},
  volume={6 5},
  pages={1233-42}
}
Perfringolysin O, a bacterial cytolytic toxin, forms unusually large pores in cholesterol-containing membranes by the spontaneous insertion of two of its four domains into the bilayer. By monitoring the kinetics of domain-specific conformational changes and pore formation using fluorescence spectroscopy, the temporal sequence of domain-membrane interactions has been established. One membrane-exposed domain does not penetrate deeply into the bilayer and is not part of the actual pore, but is… CONTINUE READING