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TitleThe structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 6977, Year 2025
Publish dateJul 29, 2025
AuthorsSasha L Evans / Iryna Peretiazhko / Sahil Y Karnani / Lindsey S Marmont / James H R Wheeler / Boo Shan Tseng / William M Durham / John C Whitney / Julien R C Bergeron /
PubMed AbstractThe Tad (Tight adherence) pilus is a bacterial appendage implicated in virulence, cell-cell aggregation, and biofilm formation. Despite its homology to the well-characterised Type IV pilus, the ...The Tad (Tight adherence) pilus is a bacterial appendage implicated in virulence, cell-cell aggregation, and biofilm formation. Despite its homology to the well-characterised Type IV pilus, the structure and assembly mechanism of the Tad pilus are poorly understood. Here, we investigate the role of the Tad pilus protein RcpC from Pseudomonas aeruginosa. Our analyses reveal that RcpC forms a dodecameric periplasmic complex, anchored to the inner membrane by a transmembrane helix, and interacting with the outer membrane secretin RcpA. We use single-particle Cryo-EM to elucidate the structure of the RcpC dodecamer, and cell-based assays to demonstrate that the RcpC-RcpA complex is essential for Tad-mediated cell-cell aggregation. Collectively, these data demonstrate that RcpC forms the Tad pilus alignment complex, which provides a conduit across the periplasm for the Tad pilus filament to access the extracellular milieu. Our experimental data and structure-based model allow us to propose a mechanism for Tad plus assembly.
External linksNat Commun / PubMed:40730569 / PubMed Central
MethodsEM (single particle)
Resolution2.45 Å
Structure data

51732

9gzr

EMDB-51732, PDB-9gzr:
Tad pilus alignment complex protein RcpC
Method: EM (single particle) / Resolution: 2.45 Å

Source
  • pseudomonas aeruginosa pao1 (bacteria)
KeywordsMEMBRANE PROTEIN / Tad pilus / Pseudomonas aeruginosa / biofilms

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