Journal article icon

Journal article

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 ...

Expand abstract

Actions


Access Document


Publisher copy:
10.1016/j.cell.2005.02.033

Authors


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

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP