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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-2-14
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pubmed:databankReference |
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pubmed:abstractText |
Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal structure of the water-soluble form of E. coli HlyE at 2.0 A resolution and the visualization of the lipid-associated form of the toxin in projection at low resolution by electron microscopy. The crystal structure reveals HlyE to be the first member of a new family of toxin structures, consisting of an elaborated helical bundle some 100 A long. The electron micrographs show how HlyE oligomerizes in the presence of lipid to form transmembrane pores. Taken together, the data from these two structural techniques allow us to propose a simple model for the structure of the pore and for membrane interaction.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemolysin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hlya protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/hlyE protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-76
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10660049-Bacterial Proteins,
pubmed-meshheading:10660049-Bacterial Toxins,
pubmed-meshheading:10660049-Conserved Sequence,
pubmed-meshheading:10660049-Crystallography, X-Ray,
pubmed-meshheading:10660049-Escherichia coli,
pubmed-meshheading:10660049-Escherichia coli Proteins,
pubmed-meshheading:10660049-Hemolysin Proteins,
pubmed-meshheading:10660049-Lipids,
pubmed-meshheading:10660049-Membrane Proteins,
pubmed-meshheading:10660049-Microscopy, Electron,
pubmed-meshheading:10660049-Molecular Sequence Data,
pubmed-meshheading:10660049-Porins,
pubmed-meshheading:10660049-Protein Structure, Quaternary,
pubmed-meshheading:10660049-Protein Structure, Secondary,
pubmed-meshheading:10660049-Protein Structure, Tertiary,
pubmed-meshheading:10660049-Salmonella typhi,
pubmed-meshheading:10660049-Sequence Homology, Amino Acid,
pubmed-meshheading:10660049-Shigella flexneri
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pubmed:year |
2000
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pubmed:articleTitle |
E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy.
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pubmed:affiliation |
The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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