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    Structural basis of chaperone function and pilus biogenesis

    Sauer, F.G. and Fütterer, K. and Pinkner, J.S. and Dodson, K.W. and Hultgren, S.J. and Waksman, Gabriel (1999) Structural basis of chaperone function and pilus biogenesis. Science 285 (5430), pp. 1058-1061. ISSN 0036-8075.

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    Abstract

    Many Gram-negative pathogens assemble architecturally and functionally diverse adhesive pili on their surfaces by the chaperone-usher pathway. Immunoglobulin-like periplasmic chaperones escort pilus subunits to the usher, a large protein complex that facilitates the translocation and assembly of subunits across the outer membrane. The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G1 β strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation. The structure of the PapD-PapK complex also suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 29 Apr 2019 15:10
    Last Modified: 29 Apr 2019 15:10
    URI: http://eprints.bbk.ac.uk/id/eprint/27349

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