- 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.
- Publisher copy:
- 10.1016/S1438-4221(00)80049-1
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2000
Journal article
Structural basis of pore formation by cholesterol-binding toxins.
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