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Structural basis of pore formation by the bacterial toxin pneumolysin.

Abstract:

The bacterial toxin pneumolysin is released as a soluble monomer that kills target cells by assembling into large oligomeric rings and forming pores in cholesterol-containing membranes. Using cryo-EM and image processing, we have determined the structures of membrane-surface bound (prepore) and inserted-pore oligomer forms, providing a direct observation of the conformational transition into the pore form of a cholesterol-dependent cytolysin. In the pore structure, the domains of the monomer ...

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Publisher copy:
10.1016/j.cell.2005.02.033

Authors


Tilley, SJ More by this author
Orlova, EV More by this author
Gilbert, RJ More by this author
Andrew, PW More by this author
Saibil, HR More by this author
Journal:
Cell
Volume:
121
Issue:
2
Pages:
247-256
Publication date:
2005-04-05
DOI:
EISSN:
1097-4172
ISSN:
0092-8674
URN:
uuid:8406fab2-7b2c-4ab2-802c-13ea65ac56f2
Source identifiers:
94673
Local pid:
pubs:94673

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