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    Dissection of pilus tip assembly by the FimD usher monomer

    Allen, William J. and Phan, Gilles and Hultgren, S.J. and Waksman, Gabriel (2013) Dissection of pilus tip assembly by the FimD usher monomer. Journal of Molecular Biology 425 (5), pp. 958-967. ISSN 0022-2836.

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    Type 1 pili are representative of a class of bacterial surface structures assembled by the conserved chaperone/usher pathway and used by uropathogenic Escherichia coli to attach to bladder cells during infection. The outer membrane assembly platform – the usher – is critical for the formation of pili, catalysing the polymerization of pilus subunits and enabling the secretion of the nascent pilus. Despite extensive structural characterisation of the usher, a number of questions about its mechanism remain, notably its oligomerization state, and how it orchestrates the ordered assembly of pilus subunits. We demonstrate here that the FimD usher is able to catalyse in vitro pilus assembly effectively in its monomeric form. Further, by establishing the kinetics of usher-catalysed reactions between various pilus subunits, we establish a complete kinetic model of tip fibrillum assembly, able to account for the order of subunits in native type 1 pili.


    Item Type: Article
    Keyword(s) / Subject(s): Uropathogenic E. coli, chaperone, membrane transporters, kinetics, fimbriae
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 09 Jan 2013 10:40
    Last Modified: 02 Aug 2023 17:01


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