Journal
SCIENCE
Volume 306, Issue 5698, Pages 1040-1042Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1102610
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Funding
- NCRR NIH HHS [P42 RR-01081] Funding Source: Medline
- NIAID NIH HHS [AI30492] Funding Source: Medline
- NIGMS NIH HHS [R01 GM066145, GM35433, GM66145] Funding Source: Medline
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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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