Aerolysin - A paradigm for membrane insertion of beta-sheet protein toxins?

Jamie Rossjohn, Susanne C. Feil, William J. McKinstry, Demetrius Tsernoglou, Gisou Van Der Goot, J. Thomas Buckley, Michael W. Parker

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50 Citations (Scopus)


The 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 proteins.

Original languageEnglish
Pages (from-to)92-100
Number of pages9
JournalJournal of Structural Biology
Issue number2
Publication statusPublished - 1 Jan 1998
Externally publishedYes


  • Aerolysin
  • Membrane channels
  • Membrane insertion
  • Protein toxins
  • X-ray crystallography

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