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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5698
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pubmed:dateCreated |
2004-11-5
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pubmed:abstractText |
Type III secretion systems (TTSSs) mediate translocation of virulence factors into host cells. We report the 17-angstrom resolution structures of a central component of Salmonella typhimurium TTSS, the needle complex, and its assembly precursor, the bacterial envelope-anchored base. Both the base and the fully assembled needle complex adopted multiple oligomeric states in vivo, and needle assembly was accompanied by recruitment of the protein PrgJ as a structural component of the base. Moreover, conformational changes during needle assembly created scaffolds for anchoring both PrgJ and the needle substructure and may provide the basis for substrate-specificity switching during type III secretion.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-10334981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-10944190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-10984518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-11018143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-11157927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-11169106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-11687484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-12093756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-12206765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-12754250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-2548211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-8751894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15528446-9554854
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
5
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pubmed:volume |
306
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1040-2
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pubmed:dateRevised |
2011-6-15
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pubmed:meshHeading |
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pubmed:year |
2004
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pubmed:articleTitle |
Structural insights into the assembly of the type III secretion needle complex.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520-8024, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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