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Structural basis of pore formation by cholesterol-binding toxins.

Abstract:
In this paper we describe reconstructions by electron cryo-microscopy of two oligomeric states of the pore-forming toxin pneumolysin. The results are interpreted by the fitting of atomic models of separated domains to the 3-dimensional electron density maps, revealing two steps in the mechanism of pore formation by the family of cholesterol-binding toxins. We briefly describe the observation of the toxin pore in model membranes and contrast the apparent mechanism of pneumolysin with that of other pore-forming toxins.

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Authors


Gilbert, RJ More by this author
Jiménez, JL More by this author
Andrew, PW More by this author
Saibil, HR More by this author
Journal:
International journal of medical microbiology : IJMM
Volume:
290
Issue:
4-5
Pages:
389-394
Publication date:
2000-10-05
DOI:
EISSN:
1618-0607
ISSN:
1438-4221
URN:
uuid:e8d7a6e5-4774-4ace-8dd9-456fe9eaa0ce
Source identifiers:
5592
Local pid:
pubs:5592

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