Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers.

@article{Goot1993OligomerizationOT,
  title={Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers.},
  author={F Gisou van der Goot and Franc Pattus and K R Wong and James Thomas Buckley},
  journal={Biochemistry},
  year={1993},
  volume={32 10},
  pages={
          2636-42
        }
}
Oligomerization is a necessary step in channel formation by the bacterial toxin aerolysin. We have identified a region of aerolysin containing two tryptophans which influence the ability of the protein to oligomerize. Changing the tryptophan at position 371 or 373 to leucine resulted in mutant proteins that oligomerized at much lower concentrations than the wild-type toxin. Near-ultraviolet circular dichroism measurements showed that the tertiary structures of the L-371 and L-373 mutant toxins… CONTINUE READING

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