The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation.

@article{Ramachandran2005TheDO,
  title={The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation.},
  author={Rajesh Ramachandran and Rodney K. Tweten and Arthur E. Johnson},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 20},
  pages={7139-44}
}
FRET measurements were used to determine the domain-specific topography of perfringolysin O, a pore-forming toxin, on a membrane surface at different stages of pore formation. The data reveal that the elongated toxin monomer binds stably to the membrane in an "end-on" orientation, with its long axis approximately perpendicular to the plane of the membrane bilayer. This orientation is largely retained even after monomer association to form an oligomeric prepore complex. The domain 3 (D3… CONTINUE READING

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