Multiple conformations facilitate PilT function in the type IV pilus

Matthew McCallum, Samir Benlekbir, Sheryl Nguyen, Stephanie Tammam, John L. Rubinstein (), Lori L. Burrows () and P. Lynne Howell ()
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Matthew McCallum: University of Toronto
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
Lori L. Burrows: McMaster University
P. Lynne Howell: University of Toronto

Nature Communications, 2019, vol. 10, issue 1, 1-16

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-13070-z

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