Rossjohn, J.Feil, S. C.McKinstry, W. J.Tsernoglou, D.van der Goot, G.Buckley, J. T.Parker, M. W.2009-02-022009-02-022009-02-02199810.1006/jsbi.1997.3947https://infoscience.epfl.ch/handle/20.500.14299/34701The determination of the crystal structure of the bacterial protein proaerolysin provided the first view of a pore-forming toxin constructed mainly from beta-sheet. The structure that was obtained and subsequent crystallographic and biochemical studies have together allowed us to explain how the toxin is transformed from a water-soluble dimer to a heptameric transmembrane pore. Recent discoveries of structural similarities between aerolysin and other toxins suggest that the structure/function studies we have made may prove useful in understanding the actions of a number of pore-forming proteinstext::journal::journal article::review article