Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state.

@article{Eifler2006CytotoxinCF,
  title={Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state.},
  author={Nora Eifler and Michael Vetsch and Marco Gregorini and Philippe Ringler and Mohamed Chami and Ansgar Philippsen and Andrea L Fritz and Shirley A. M{\"u}ller and Rudi Glockshuber and Andreas H. Engel and Ulla Grauschopf},
  journal={The EMBO journal},
  year={2006},
  volume={25 11},
  pages={2652-61}
}
ClyA is a pore-forming toxin from virulent Escherichia coli and Salmonella enterica strains. Here, we show that the intrinsic hemolytic activity of ClyA is independent of its redox state, and that the assembly of both reduced and oxidized ClyA to the ring-shaped oligomer is triggered by contact with lipid or detergent. A rate-limiting conformational transition in membrane-bound ClyA monomers precedes their assembly to the functional pore. We obtained a three-dimensional model of the detergent… CONTINUE READING

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