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TitleStructural insights into the assembly of the type III secretion needle complex.
Journal, issue, pagesScience, Vol. 306, Issue 5698, Page 1040-1042, Year 2004
Publish dateNov 5, 2004
AuthorsThomas C Marlovits / Tomoko Kubori / Anand Sukhan / Dennis R Thomas / Jorge E Galán / Vinzenz M Unger /
PubMed AbstractType 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, ...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.
External linksScience / PubMed:15528446 / PubMed Central
MethodsEM (single particle)
Resolution17.0 - 19.0 Å
Structure data

EMDB-1100:
Structural insights into the assembly of the type III secretion needle complex.
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-1224:
Structural insights into the assembly of the type III secretion needle complex.
Method: EM (single particle) / Resolution: 19.0 Å

Source
  • Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)
  • Salmonella tyhpimurium

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