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- EMDB-28152: Cryo-EM reconstruction of the CS20 bacterial adhesion pili -

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Basic information

Entry
Database: EMDB / ID: EMD-28152
TitleCryo-EM reconstruction of the CS20 bacterial adhesion pili
Map dataPrimary map.
Sample
  • Organelle or cellular component: CS20 bacterial adhesion pili
    • Protein or peptide: CS20 fimbria major subunit protein
Function / homologyFimbrial-type adhesion domain superfamily / Adhesion domain superfamily / pilus / cell adhesion / CS20 fimbria major subunit protein
Function and homology information
Biological speciesEscherichia coli (E. coli)
Methodhelical reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsDoran MH / Bullitt E
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)1R21AI156236-01 United States
CitationJournal: Structure / Year: 2023
Title: Three structural solutions for bacterial adhesion pilus stability and superelasticity.
Authors: Matthew H Doran / Joseph L Baker / Tobias Dahlberg / Magnus Andersson / Esther Bullitt /
Abstract: Bacterial adhesion pili are key virulence factors that mediate host-pathogen interactions in diverse epithelial environments. Deploying a multimodal approach, we probed the structural basis ...Bacterial adhesion pili are key virulence factors that mediate host-pathogen interactions in diverse epithelial environments. Deploying a multimodal approach, we probed the structural basis underpinning the biophysical properties of pili originating from enterotoxigenic (ETEC) and uropathogenic bacteria. Using cryo-electron microscopy we solved the structures of three vaccine target pili from ETEC bacteria, CFA/I, CS17, and CS20. Pairing these and previous pilus structures with force spectroscopy and steered molecular dynamics simulations, we find a strong correlation between subunit-subunit interaction energies and the force required for pilus unwinding, irrespective of genetic similarity. Pili integrate three structural solutions for stabilizing their assemblies: layer-to-layer interactions, N-terminal interactions to distant subunits, and extended loop interactions from adjacent subunits. Tuning of these structural solutions alters the biophysical properties of pili and promotes the superelastic behavior that is essential for sustained bacterial attachment.
History
DepositionSep 14, 2022-
Header (metadata) releaseMar 22, 2023-
Map releaseMar 22, 2023-
UpdateMay 17, 2023-
Current statusMay 17, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_28152.png

Downloads & links

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Map

FileDownload / File: emd_28152.map.gz / Format: CCP4 / Size: 32.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPrimary map.
Voxel sizeX=Y=Z: 1.078 Å
Density
Contour LevelBy AUTHOR: 0.0295
Minimum - Maximum-0.117192045 - 0.19898307
Average (Standard dev.)0.00013409976 (±0.009488511)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions204204204
Spacing204204204
CellA=B=C: 219.91199 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_28152_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2.

Fileemd_28152_half_map_1.map
AnnotationHalf map 2.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 1.

Fileemd_28152_half_map_2.map
AnnotationHalf map 1.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : CS20 bacterial adhesion pili

EntireName: CS20 bacterial adhesion pili
Components
  • Organelle or cellular component: CS20 bacterial adhesion pili
    • Protein or peptide: CS20 fimbria major subunit protein

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Supramolecule #1: CS20 bacterial adhesion pili

SupramoleculeName: CS20 bacterial adhesion pili / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (E. coli) / Strain: WS7179A

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Macromolecule #1: CS20 fimbria major subunit protein

MacromoleculeName: CS20 fimbria major subunit protein / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 17.435199 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
APAANDSSQA TLNFSGRVTS SLCQVKTDDL VKNISLGEVS KSALEATGKS PAQSFQVNLI NCDSLTDDIS YVLADANNNG TTTAYLVPK SGDTAATGVG VFVETSKGTP VNIGSDQKLD VVANKGNALS EQVIPLRAYI GTQTRAAGAI GTDVTAGTVD A TGVLTIRA ADAT

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statehelical array

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Sample preparation

BufferpH: 7.4
GridModel: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 400 / Support film - Material: GOLD / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. / Details: 15 mA using the Pelco EasiGlow machine
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK III

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number real images: 5236 / Average electron dose: 53.62 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Segment selectionNumber selected: 9590890 / Software - Name: RELION (ver. 3.1.1)
Startup modelType of model: OTHER / Details: solid featureless cylinder
Final angle assignmentType: NOT APPLICABLE / Software - Name: RELION (ver. 3.1.1)
Final reconstructionApplied symmetry - Helical parameters - Δz: 8.953 Å
Applied symmetry - Helical parameters - Δ&Phi: 111.84 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 88048
FSC plot (resolution estimation)

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