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

Research output: Contribution to journalArticlepeer-review

282 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 languageEnglish (US)
Pages (from-to)1040-1042
Number of pages3
JournalScience
Volume306
Issue number5698
DOIs
StatePublished - Nov 5 2004

ASJC Scopus subject areas

  • General

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