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TitleThe Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.
Journal, issue, pagesStructure, Vol. 25, Issue 12, Page 1829-11838.e4, Year 2017
Publish dateDec 5, 2017
AuthorsManuela K Hospenthal / Dawid Zyla / Tiago R D Costa / Adam Redzej / Christoph Giese / James Lillington / Rudi Glockshuber / Gabriel Waksman /
PubMed AbstractAdhesive 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 ...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.
External linksStructure / PubMed:29129382 / PubMed Central
MethodsEM (helical sym.)
Resolution4.2 Å
Structure data

3809

5oh0

EMDB-3809, PDB-5oh0:
The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod
Method: EM (helical sym.) / Resolution: 4.2 Å

Source
  • escherichia coli j96 (bacteria)
KeywordsPROTEIN FIBRIL / bacterial pilus / chaperone-usher pilus

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