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    Structural and energetic basis of folded-protein transport by the FimD usher

    Geibel, Sebastien and Procko, E. and Hultgren, S.J. and Baker, D. and Waksman, Gabriel (2013) Structural and energetic basis of folded-protein transport by the FimD usher. Nature 496 (7444), pp. 243-246. ISSN 0028-0836.

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    Abstract

    Type 1 pili, produced by uropathogenic Escherichia coli, are multisubunit fibres crucial in recognition of and adhesion to host tissues1. During pilus biogenesis, subunits are recruited to an outer membrane assembly platform, the FimD usher, which catalyses their polymerization and mediates pilus secretion2. The recent determination of the crystal structure of an initiation complex provided insight into the initiation step of pilus biogenesis resulting in pore activation, but very little is known about the elongation steps that follow3. Here, to address this question, we determine the structure of an elongation complex in which the tip complex assembly composed of FimC, FimF, FimG and FimH passes through FimD. This structure demonstrates the conformational changes required to prevent backsliding of the nascent pilus through the FimD pore and also reveals unexpected properties of the usher pore. We show that the circular binding interface between the pore lumen and the folded substrate participates in transport by defining a low-energy pathway along which the nascent pilus polymer is guided during secretion.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Structural biology
    School: School of Science > Biological Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 15 Apr 2013 06:43
    Last Modified: 06 Dec 2016 10:46
    URI: https://eprints.bbk.ac.uk/id/eprint/6464

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