Structure and dynamics of a pore-forming toxin

Our work, in collaboration with the Zuber and Posthaus groups in the University of Bern, was just published in EMBO Reports (well done Julia Bruggisser and Ioan Iacovache for the beautiful cover image!).

We investigated the structure, dynamics, and properties beta-toxin, a protein part of the offensive arsenal of Clostridium perfringes bacteria. This protein assembles according to a unique architecture, featuring beta-barrels at both ends. Calculations from Samuel Musson on the newly discovered atomic structure reveal that the toxin should be marginally selective to cations, and that the solvent-exposed barrel is remarkably flexible.

We conclude that beta-toxin could be suitable candidate for small molecule sensing or selective molecule delivery and transport.

Reference:  J. Bruggisser, I. Iacovache, S. C. Musson, M. T. Degiacomi, H. Posthaus, B. Zuber (2022). Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin, Embo Reports

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