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TitleThe assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3032, Year 2024
Publish dateApr 8, 2024
AuthorsDawid S Zyla / Thomas Wiegand / Paul Bachmann / Rafal Zdanowicz / Christoph Giese / Beat H Meier / Gabriel Waksman / Manuela K Hospenthal / Rudi Glockshuber /
PubMed AbstractType 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of ...Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA and is assembled in vivo by the assembly platform FimD. Although type 1 pilus rods can self-assemble from FimA in vitro, this reaction is slower and produces structures with lower kinetic stability against denaturants compared to in vivo-assembled rods. Our study reveals that FimD-catalysed in vitro-assembled type 1 pilus rods attain a similar stability as pilus rods assembled in vivo. Employing structural, biophysical and biochemical analyses, we show that in vitro assembly reactions lacking FimD produce pilus rods with structural defects, reducing their stability against dissociation. Overall, our results indicate that FimD is not only required for the catalysis of pilus assembly, but also to control the assembly of the most stable quaternary structure.
External linksNat Commun / PubMed:38589417 / PubMed Central
MethodsEM (helical sym.)
Resolution2.52 - 2.85 Å
Structure data

10721

6y7s

EMDB-10721, PDB-6y7s:
2.85 A cryo-EM structure of the in vivo assembled type 1 pilus rod
Method: EM (helical sym.) / Resolution: 2.85 Å

17863

8psv

EMDB-17863, PDB-8psv:
2.7 A cryo-EM structure of in vitro assembled type 1 pilus rod
Method: EM (helical sym.) / Resolution: 2.7 Å

17878

8ptu

EMDB-17878, PDB-8ptu:
2.5 A cryo-EM structure of the in vitro FimD-catalyzed assembly of type 1 pilus rod
Method: EM (helical sym.) / Resolution: 2.52 Å

Source
  • escherichia coli (E. coli)
KeywordsSTRUCTURAL PROTEIN / FimA / pilus / monomer / subunit / pili / main structural subunit / high resolution / cryo-EM / helical processing / RELION / Chaperone-usher pilus

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