Structural basis for usher activation and intramolecular subunit transfer in P pilus biogenesis in Escherichia coli.

ABSTRACT: Chaperone-usher pathway pili are extracellular proteinaceous fibres ubiquitously found on Gram-negative bacteria, and mediate host-pathogen interactions and biofilm formation critical in pathogenesis in numerous human diseases¹. During pilus assembly, an outer membrane macromolecular machine called the usher catalyses pilus biogenesis from the individual subunits that are delivered as chaperone-subunit complexes in the periplasm. The usher orchestrates pilus assembly using all five functional domains: a 24-stranded transmembrane β-barrel translocation domain, a β-sandwich plug domain, an amino-terminal periplasmic domain and two carboxy-terminal periplasmic domains (CTD1 and CTD2)^2-6. Despite extensive structural and functional characterization, the mechanism by which

SUBMITTER: Omattage NS 

PROVIDER: S-EPMC6258349 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature