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J Struct Biol. 1998;121(2):92-100.

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

Author information

1
Ian Potter Foundation Protein Crystallography Laboratory, St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.

Abstract

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.

PMID:
9615432
DOI:
10.1006/jsbi.1997.3947
[Indexed for MEDLINE]

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