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, 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.
Original language | English (US) |
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Pages (from-to) | 1040-1042 |
Number of pages | 3 |
Journal | Science |
Volume | 306 |
Issue number | 5698 |
DOIs | |
State | Published - Nov 5 2004 |
ASJC Scopus subject areas
- General