Increased stability upon heptamerization of the pore-forming toxin aerolysin.

doi:10.1074/jbc.274.51.36722

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Article

Increased stability upon heptamerization of the pore-forming toxin aerolysin.

The Journal of biological chemistry - 17 Dec 1999

Lesieur C, Frutiger S, Hughes G, Kellner R, Pattus F, van der Goot F G

Abstract excerpt

Aerolysin is a bacterial pore-forming toxin that is secreted as an inactive precursor, which is then processed at its COOH terminus and finally forms a circular heptameric ring which inserts into membranes to form a pore. We have analyzed the stability of the precursor proaerolysin and the heptameric complex. Equilibrium unfolding induced by urea and guanidinium hydrochloride was monitored by measuring the...

Topics

Amino Acid Sequence
Bacterial Toxins
Dimerization
Molecular Sequence Data
Mutation
Pore Forming Cytotoxic Proteins
Protein Conformation
Protein Denaturation
Urea

Source

Open in PubMed

Identifiers

PMID: 10593978
DOI: 10.1074/jbc.274.51.36722

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