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-Structure paper
Title | Structural insights into the assembly of the type III secretion needle complex. |
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Journal, issue, pages | Science, Vol. 306, Issue 5698, Page 1040-1042, Year 2004 |
Publish date | Nov 5, 2004 |
![]() | Thomas C Marlovits / Tomoko Kubori / Anand Sukhan / Dennis R Thomas / Jorge E Galán / Vinzenz M Unger / ![]() |
PubMed Abstract | 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, ...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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Methods | EM (single particle) |
Resolution | 17.0 - 19.0 Å |
Structure data | ![]() EMDB-1100: ![]() EMDB-1224: |
Source |
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