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

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.

SUBMITTER: Marlovits TC

PROVIDER: S-EPMC1459965 | biostudies-literature | 2004 Nov

REPOSITORIES: biostudies-literature

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

Marlovits Thomas C TC Kubori Tomoko T Sukhan Anand A Thomas Dennis R DR Galán Jorge E JE Unger Vinzenz M VM

Science (New York, N.Y.) 20041101 5698

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, ...[more]

PMID: 15528446

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2018-10-16 | PXD010239 | Pride

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