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Multiple conformations facilitate PilT function in the type IV pilus

Author

Listed:
  • Matthew McCallum

    (University of Toronto
    The Hospital for Sick Children)

  • Samir Benlekbir

    (The Hospital for Sick Children)

  • Sheryl Nguyen

    (The Hospital for Sick Children)

  • Stephanie Tammam

    (The Hospital for Sick Children)

  • John L. Rubinstein

    (University of Toronto
    The Hospital for Sick Children
    University of Toronto)

  • Lori L. Burrows

    (McMaster University)

  • P. Lynne Howell

    (University of Toronto
    The Hospital for Sick Children)

Abstract

Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by motor ATPases of the PilT/VirB11-like family. This family is thought to operate with C2 symmetry; however, most of these ATPases crystallize with either C3 or C6 symmetric conformations. The relevance of these conformations is unclear. Here, we determine the X-ray structures of PilT in four unique conformations and use these structures to classify the conformation of available PilT/VirB11-like family member structures. Single particle electron cryomicroscopy (cryoEM) structures of PilT reveal condition-dependent preferences for C2, C3, and C6 conformations. The physiologic importance of these conformations is validated by coevolution analysis and functional studies of point mutants, identifying a rare gain-of-function mutation that favours the C2 conformation. With these data, we propose a comprehensive model of PilT function with broad implications for PilT/VirB11-like family members.

Suggested Citation

  • Matthew McCallum & Samir Benlekbir & Sheryl Nguyen & Stephanie Tammam & John L. Rubinstein & Lori L. Burrows & P. Lynne Howell, 2019. "Multiple conformations facilitate PilT function in the type IV pilus," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13070-z
    DOI: 10.1038/s41467-019-13070-z
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    Cited by:

    1. Michael Hohl & Emma J. Banks & Max P. Manley & Tung B. K. Le & Harry H. Low, 2024. "Bidirectional pilus processing in the Tad pilus system motor CpaF," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Shuaiqi Guo & Yunjie Chang & Yves V. Brun & P. Lynne Howell & Lori L. Burrows & Jun Liu, 2024. "PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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