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 C_2, C₃, and C<

SUBMITTER: McCallum M 

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

REPOSITORIES: biostudies-literature