Journal article
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 …
Authors
McCallum M; Benlekbir S; Nguyen S; Tammam S; Rubinstein JL; Burrows LL; Howell PL
Journal
Nature Communications, Vol. 10, No. 1,
Publisher
Springer Nature
DOI
10.1038/s41467-019-13070-z
ISSN
2041-1723