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

Thomas C. Marlovits; Tomoko Kubori; Anand Sukhan; Dennis R. Thomas; Jorge E. Galán; Vinzenz M. Unger

doi:10.1126/science.1102610

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

Thomas C. Marlovits, Tomoko Kubori, Anand Sukhan, Dennis R. Thomas, Jorge E. Galán, Vinzenz M. Unger^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

308 Scopus citations

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)
Pages (from-to)	1040-1042
Number of pages	3
Journal	Science
Volume	306
Issue number	5698
DOIs	https://doi.org/10.1126/science.1102610
State	Published - Nov 5 2004

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title = "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.",

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AU - Marlovits, Thomas C.

AU - Kubori, Tomoko

AU - Sukhan, Anand

AU - Thomas, Dennis R.

AU - Galán, Jorge E.

AU - Unger, Vinzenz M.

PY - 2004/11/5

Y1 - 2004/11/5

N2 - 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.

AB - 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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Structural insights into the assembly of the type III secretion needle complex

Abstract

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