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Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination

Author

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  • Paul Bachmann

    (ETH Zürich)

  • Pavel Afanasyev

    (ETH Zürich)

  • Daniel Boehringer

    (ETH Zürich)

  • Rudi Glockshuber

    (ETH Zürich)

Abstract

Uropathogenic Escherichia coli strains use filamentous type 1 pili to adhere to and invade uroepithelial cells. The pilus consists of a flexible tip fibrillum, formed by the adhesin FimH and the subunits FimG and FimF. The pilus rod is a helical assembly of up to 3000 copies of the main subunit FimA, terminated by a single copy of the subunit FimI that anchors the rod to the assembly platform FimD in the outer membrane. Although type 1 pilus assembly can be completely reconstituted in vitro, the precise mechanism of assembly termination on FimD is still unknown. Here, we present cryo-electron microscopy structures of the fully assembled pilus with all its components prior to and after incorporation of FimI, capped with the assembly chaperone FimC. The structures reveal that FimD positions the proximal end of the pilus rod at an angle of ca. 50 degrees relative to the plane of the outer membrane. Specific interactions between FimI and FimC, absent in the equivalent FimA-FimC interface of the non-terminated pilus, stabilize the assembly-terminated state. In addition, we present structures of the transition region between the tip fibrillum and the helical rod, showing how FimF aligns the tip fibrillum along the rod axis.

Suggested Citation

  • Paul Bachmann & Pavel Afanasyev & Daniel Boehringer & Rudi Glockshuber, 2025. "Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination," Nature Communications, Nature, vol. 16(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60325-z
    DOI: 10.1038/s41467-025-60325-z
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    References listed on IDEAS

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    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. Natalia Pakharukova & Henri Malmi & Minna Tuittila & Tobias Dahlberg & Debnath Ghosal & Yi-Wei Chang & Si Lhyam Myint & Sari Paavilainen & Stefan David Knight & Urpo Lamminmäki & Bernt Eric Uhlin & Ma, 2022. "Archaic chaperone–usher pili self-secrete into superelastic zigzag springs," Nature, Nature, vol. 609(7926), pages 335-340, September.
    3. Maximilian M. Sauer & Roman P. Jakob & Jonathan Eras & Sefer Baday & Deniz Eriş & Giulio Navarra & Simon Bernèche & Beat Ernst & Timm Maier & Rudi Glockshuber, 2016. "Catch-bond mechanism of the bacterial adhesin FimH," Nature Communications, Nature, vol. 7(1), pages 1-13, April.
    4. Alvaro Alonso-Caballero & Jörg Schönfelder & Simon Poly & Fabiano Corsetti & David Sancho & Emilio Artacho & Raul Perez-Jimenez, 2018. "Mechanical architecture and folding of E. coli type 1 pilus domains," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    5. Michael Vetsch & Chasper Puorger & Thomas Spirig & Ulla Grauschopf & Eilika U. Weber-Ban & Rudi Glockshuber, 2004. "Pilus chaperones represent a new type of protein-folding catalyst," Nature, Nature, vol. 431(7006), pages 329-333, September.
    6. 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.
    7. Gilles Phan & Han Remaut & Tao Wang & William J. Allen & Katharina F. Pirker & Andrey Lebedev & Nadine S. Henderson & Sebastian Geibel & Ender Volkan & Jun Yan & Micha B. A. Kunze & Jerome S. Pinkner , 2011. "Crystal structure of the FimD usher bound to its cognate FimC–FimH substrate," Nature, Nature, vol. 474(7349), pages 49-53, June.
    8. 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.
    9. Minge Du & Zuanning Yuan & Hongjun Yu & Nadine Henderson & Samema Sarowar & Gongpu Zhao & Glenn T. Werneburg & David G. Thanassi & Huilin Li, 2018. "Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD," Nature, Nature, vol. 562(7727), pages 444-447, October.
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