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- EMDB-51732: Tad pilus alignment complex protein RcpC -

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Basic information

Entry
Database: EMDB / ID: EMD-51732
TitleTad pilus alignment complex protein RcpC
Map data
Sample
  • Complex: Dodecameric assembly of RcpC
    • Protein or peptide: RcpC
KeywordsTad pilus / Pseudomonas aeruginosa / membrane protein / 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)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.45 Å
AuthorsEvans SL / Peretiazhko I / Bergeron JRC
Funding support France, United Kingdom, 2 items
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, 2024-
Header (metadata) releaseMay 21, 2025-
Map releaseMay 21, 2025-
UpdateAug 13, 2025-
Current statusAug 13, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51732.png

Downloads & links

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Map

FileDownload / File: emd_51732.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 300 pix.
= 255. Å		0.85 Å/pix.
x 300 pix.
= 255. Å		0.85 Å/pix.
x 300 pix.
= 255. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.85 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0574
Minimum - Maximum-0.0019689705 - 1.7239542
Average (Standard dev.)0.00241366 (±0.035540517)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 255.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_51732_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_51732_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Dodecameric assembly of RcpC

EntireName: Dodecameric assembly of RcpC
Components
  • Complex: Dodecameric assembly of RcpC
    • Protein or peptide: RcpC

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Supramolecule #1: Dodecameric assembly of RcpC

SupramoleculeName: Dodecameric assembly of RcpC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)
Molecular weightTheoretical: 412 KDa

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Macromolecule #1: RcpC

MacromoleculeName: RcpC / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)
Molecular weightTheoretical: 29.816893 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MNAHAPSVAP ASATVDASLE KLERKPVLVA SRDLPALAVI GRDDLSVELL RTAPVGSYDR PEALLGKRVW VAVPAGSILS AATLEPGGP LARTIRPDER AMAIAVDEVV GGGGFVLPGD YVDVMLFVRD ERDGESTPLA QLVLPGVRVL TYGERIAVGS D GQDRSNQE ...String:
MNAHAPSVAP ASATVDASLE KLERKPVLVA SRDLPALAVI GRDDLSVELL RTAPVGSYDR PEALLGKRVW VAVPAGSILS AATLEPGGP LARTIRPDER AMAIAVDEVV GGGGFVLPGD YVDVMLFVRD ERDGESTPLA QLVLPGVRVL TYGERIAVGS D GQDRSNQE KDPRPPRTAV LAVPEDGVAR LMLASQAGSL RLAIRSKDEE LYRREQEGAL LQASLGAPSA ALSLDQLLER RK PTAPSVR SAAPRVPVAN GVTVYRGSAM THEAPLEHHH HHH

UniProtKB: RcpC

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 8
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 60 sec.
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number real images: 14847 / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 14150712
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.45 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1108916
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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