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Structural analysis of the protein/lipid complexes associated with pore formation by the bacterial toxin pneumolysin.

Abstract:

Pneumolysin, a major virulence factor of the human pathogen Streptococcus pneumoniae, is a soluble protein that disrupts cholesterol-containing membranes of cells by forming ring-shaped oligomers. Magic angle spinning and wideline static (31)P NMR have been used in combination with freeze-fracture electron microscopy to investigate the effect of pneumolysin on fully hydrated model membranes containing cholesterol and phosphatidylcholine and dicetyl phosphate (10:10:1 molar ratio). NMR spectra...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.M005126200

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Biology
Andrew, PW More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
The Journal of biological chemistry
Volume:
276
Issue:
8
Pages:
5714-5719
Publication date:
2001-02-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:d677a2d9-8934-4fff-bb9a-66e2e825f9e5
Source identifiers:
8457
Local pid:
pubs:8457

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