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

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


Published in:
J Struct Biol, 121, 2, 92-100
Year:
1998
Note:
Author address: Ian Potter Foundation Protein Crystallography Laboratory, St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia
Laboratories:




 Record created 2009-02-02, last modified 2018-09-13


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