pubmed-article:10660049 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:10660049 | lifeskim:mentions | umls-concept:C1325742 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0019053 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0302523 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0700325 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0026019 | lld:lifeskim |
pubmed-article:10660049 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
pubmed-article:10660049 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:10660049 | pubmed:dateCreated | 2000-2-14 | lld:pubmed |
pubmed-article:10660049 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10660049 | 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. | lld:pubmed |
pubmed-article:10660049 | pubmed:language | eng | lld:pubmed |
pubmed-article:10660049 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10660049 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10660049 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10660049 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10660049 | pubmed:month | Jan | lld:pubmed |
pubmed-article:10660049 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:GreenJJ | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:AtkinsAA | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:ArtymiukP JPJ | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:StillmanT JTJ | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:BulloughP APA | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:WallaceA JAJ | lld:pubmed |
pubmed-article:10660049 | pubmed:author | pubmed-author:JamiesonS JSJ | lld:pubmed |
pubmed-article:10660049 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10660049 | pubmed:day | 21 | lld:pubmed |
pubmed-article:10660049 | pubmed:volume | 100 | lld:pubmed |
pubmed-article:10660049 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10660049 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10660049 | pubmed:pagination | 265-76 | lld:pubmed |
pubmed-article:10660049 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:10660049 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10660049 | pubmed:articleTitle | E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy. | lld:pubmed |
pubmed-article:10660049 | pubmed:affiliation | The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, United Kingdom. | lld:pubmed |
pubmed-article:10660049 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10660049 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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