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Science. 2004 Nov 5;306(5698):1040-2.

Structural insights into the assembly of the type III secretion needle complex.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520-8024, USA.

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.

PMID:
15528446
PMCID:
PMC1459965
DOI:
10.1126/science.1102610
[Indexed for MEDLINE]
Free PMC Article

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