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  • Title: Structural insights into the assembly of the type III secretion needle complex.
    Author: Marlovits TC, Kubori T, Sukhan A, Thomas DR, Galán JE, Unger VM.
    Journal: Science; 2004 Nov 05; 306(5698):1040-2. PubMed ID: 15528446.
    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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