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

Author

Listed:
  • Sebastian Geibel

    (Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK)

  • Erik Procko

    (University of Washington)

  • Scott J. Hultgren

    (Washington University School of Medicine)

  • David Baker

    (University of Washington)

  • Gabriel Waksman

    (Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK)

Abstract

The crystal structure of the FimD usher traversed by the tip complex of a type 1 pilus demonstrates the mechanism by which pilus subunits are assembled and translocated during pilus elongation.

Suggested Citation

  • Sebastian Geibel & Erik Procko & Scott J. Hultgren & David Baker & Gabriel Waksman, 2013. "Structural and energetic basis of folded-protein transport by the FimD usher," Nature, Nature, vol. 496(7444), pages 243-246, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7444:d:10.1038_nature12007
    DOI: 10.1038/nature12007
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    Cited by:

    1. Christoph Giese & Chasper Puorger & Oleksandr Ignatov & Zuzana Bečárová & Marco E. Weber & Martin A. Schärer & Guido Capitani & Rudi Glockshuber, 2023. "Stochastic chain termination in bacterial pilus assembly," Nature Communications, Nature, vol. 14(1), pages 1-21, December.
    2. Dawid S. Zyla & Thomas Wiegand & Paul Bachmann & Rafal Zdanowicz & Christoph Giese & Beat H. Meier & Gabriel Waksman & Manuela K. Hospenthal & Rudi Glockshuber, 2024. "The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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