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    The Cryoelectron Microscopy structure of the Type 1 Chaperone-Usher Pilus Rod

    Hospenthal, Manuela K. and Zyla, D. and Costa, Tiago R.D. and Redzej, Adam and Giese, C. and Lillington, James and Glockshuber, R. and Waksman, Gabriel (2017) The Cryoelectron Microscopy structure of the Type 1 Chaperone-Usher Pilus Rod. Structure 25 (12), 1829-1838.e4. ISSN 0969-2126.

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    Abstract

    Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable “spring-like” properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): chaperone, pilus, usher, chaperone-usher pilus, type 1 pilus, cryo-EM, pilus rod, quaternary structure, FimA, unfolding kinetics
    School: School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 14 May 2018 10:17
    Last Modified: 26 Jun 2020 06:30
    URI: https://eprints.bbk.ac.uk/id/eprint/22411

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