The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod

Open access
Author
Zyla, Dawid
Costa, Tiago R.D.
Redzej, Adam
Giese, Christoph
Lillington, James
Glockshuber, Rudi
Waksman, Gabriel
Date
2017-12-05Type
- Journal Article
Citations
Cited 9 times in
Web of Science
Cited 13 times in
Scopus
ETH Bibliography
yes
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Abstract
Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable “spring-like” properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000221817Publication status
publishedJournal / series
StructureVolume
Pages / Article No.
Publisher
Cell PressSubject
chaperone; pilus; usher; chaperone-usher pilus; type 1 pilus; cryo-EM; pilus rod; quaternary structure; FimA; unfolding kineticsOrganisational unit
03412 - Glockshuber, Rudolf / Glockshuber, Rudolf
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Show all metadata
Citations
Cited 9 times in
Web of Science
Cited 13 times in
Scopus
ETH Bibliography
yes
Altmetrics