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

Authors
  • Hospenthal, Manuela K1
  • Zyla, Dawid2
  • Costa, Tiago R D1
  • Redzej, Adam1
  • Giese, Christoph2
  • Lillington, James1
  • Glockshuber, Rudi2
  • Waksman, Gabriel3
  • 1 Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London WC1E 7HX, UK.
  • 2 Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology Zurich, Otto-Stern-Weg 5, 8093 Zurich, Switzerland. , (Switzerland)
  • 3 Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London WC1E 7HX, UK. Electronic address: [email protected]
Type
Published Article
Journal
Structure
Publisher
Elsevier
Publication Date
Dec 05, 2017
Volume
25
Issue
12
Identifiers
DOI: 10.1016/j.str.2017.10.004
PMID: 29129382
Source
Medline
Keywords
License
Unknown

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.

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