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- PDB-9gzr: Tad pilus alignment complex protein RcpC -

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Basic information

Entry
Database: PDB / ID: 9gzr
TitleTad pilus alignment complex protein RcpC
ComponentsRcpC
KeywordsMEMBRANE PROTEIN / Tad pilus / Pseudomonas aeruginosa / biofilms
Function / homologyPilus assembly, Flp-type CpaB / Flp pilus assembly protein RcpC/CpaB domain / Flp pilus assembly protein RcpC/CpaB / SAF domain / SAF / SAF domain / RcpC
Function and homology information
Biological speciesPseudomonas aeruginosa PAO1 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.45 Å
AuthorsEvans, S.L. / Peretiazhko, I. / Bergeron, J.R.C.
Funding support France, United Kingdom, 2items
OrganizationGrant numberCountry
Human Frontier Science Program (HFSP)RGY0080/2021 France
Biotechnology and Biological Sciences Research Council (BBSRC)BB/R009759/2 United Kingdom
CitationJournal: Nat Commun / Year: 2025
Title: The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.
Authors: Sasha 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 /
Abstract: 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 ...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.
History
DepositionOct 4, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 21, 2025Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Aug 13, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RcpC
B: RcpC
C: RcpC
D: RcpC
E: RcpC
F: RcpC
G: RcpC
H: RcpC
I: RcpC
J: RcpC
K: RcpC
L: RcpC


Theoretical massNumber of molelcules
Total (without water)357,80312
Polymers357,80312
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
RcpC


Mass: 29816.893 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria) / Gene: rcpC, PA4305 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HW95
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Dodecameric assembly of RcpC / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.412 MDa / Experimental value: YES
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm
Specimen holderCryogen: NITROGEN
Image recordingElectron dose: 45 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 14847

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Processing

EM softwareName: PHENIX / Version: 1.21.1_5286 / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 14150712
3D reconstructionResolution: 2.45 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1108916 / Symmetry type: POINT
RefinementHighest resolution: 2.45 Å / Cross valid method: NONE
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00317991
ELECTRON MICROSCOPYf_angle_d0.5924438
ELECTRON MICROSCOPYf_dihedral_angle_d7.3462701
ELECTRON MICROSCOPYf_chiral_restr0.0432885
ELECTRON MICROSCOPYf_plane_restr0.0063244

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