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Multiple conformations facilitate PilT function in the type IV pilus.


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.

SUBMITTER: McCallum M 

PROVIDER: S-EPMC6858323 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Multiple conformations facilitate PilT function in the type IV pilus.

McCallum Matthew M   Benlekbir Samir S   Nguyen Sheryl S   Tammam Stephanie S   Rubinstein John L JL   Burrows Lori L LL   Howell P Lynne PL  

Nature communications 20191115 1


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 C<sub>2</sub> symmetry; however, most of these ATPases crystallize with either C<sub>3</sub> or C<sub>6</sub> symmetric conformations. The relevance of these conformations is unclear. Here, we determine the X-ray struc  ...[more]

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