The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism

Marcus Mueller, Ulla Grauschopf, Timm Maier, Rudi Glockshuber and Nenad Ban ()
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Marcus Mueller: Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
Ulla Grauschopf: Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
Timm Maier: Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
Rudi Glockshuber: Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
Nenad Ban: Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland

Nature, 2009, vol. 459, issue 7247, 726-730

Abstract: α-helical toxin assembly Some toxins exert cytotoxicity by assembling into multimeric pores in the membranes of their host cells. The bacterial α-helical toxin cytolysin A, responsible for the haemolytic phenotype of several Escherichia coli and Salmonella enterica strains, is one such pore-forming toxin, whose soluble structure is known. Here Mueller et al. describe the structure of its assembled dodecameric pore. The authors propose a sequential mechanism for the large rearrangements that the monomers undergo to form the α-helical pore.

Date: 2009
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DOI: 10.1038/nature08026

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