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- EMDB-26546: Cryo-EM of self-assembled cannula CanA -

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Basic information

Entry
Database: EMDB / ID: EMD-26546
TitleCryo-EM of self-assembled cannula CanA
Map dataCryo-EM of self-assembled cannula CanA
Sample
  • Complex: CanA
    • Protein or peptide: CanA
  • Ligand: CALCIUM ION
  • Ligand: water
Keywordsself-assemble / cannula / helical tube / donor strand / PROTEIN FIBRIL
Biological speciesPyrodictium abyssi (archaea)
Methodhelical reconstruction / cryo EM / Resolution: 2.6 Å
AuthorsWang F / Miller JG / Egelman EH / Conticello VP
Funding support United States, 3 items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)NSF-DMR-1533958 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM122510 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)K99GM138756 United States
CitationJournal: Nat Commun / Year: 2025
Title: Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae.
Authors: Mike Sleutel / Ravi R Sonani / Jessalyn G Miller / Fengbin Wang / Andres Gonzalez Socorro / Yang Chen / Reece Martin / Borries Demeler / Michael J Rudolph / Vikram Alva / Han Remaut / Edward ...Authors: Mike Sleutel / Ravi R Sonani / Jessalyn G Miller / Fengbin Wang / Andres Gonzalez Socorro / Yang Chen / Reece Martin / Borries Demeler / Michael J Rudolph / Vikram Alva / Han Remaut / Edward H Egelman / Vincent P Conticello /
Abstract: Cannulae are structurally rigid tubular protein filaments that accumulate on the extracellular surface of archaea within the family Pyrodictiaceae during cell growth. These obligate anaerobes ...Cannulae are structurally rigid tubular protein filaments that accumulate on the extracellular surface of archaea within the family Pyrodictiaceae during cell growth. These obligate anaerobes propagate under hyperthermophilic conditions in which cannulae form a biomatrix that interconnects and sustains cells. The persistence of cannulae in this environment suggests that these filaments display significant thermostability, which has attracted technological interest in their development as synthetic protein-based biomaterials. Here, we report cryoEM structural analyses of ex vivo and in vitro assembled recombinant cannulae. We demonstrate that the interactions between protomers in native and recombinant cannulae is based on donor strand complementation (DSC), a form of non-covalent polymerization previously observed for bacterial chaperone-usher pili. Unexpectedly, calcium ion coordination at the subunit interfaces reinforces the network of donor strand interactions in the cannulae. This study provides insight into the mechanism of assembly of cannulae and the structural origin of their high stability and rigidity.
History
DepositionMar 29, 2022-
Header (metadata) releaseApr 12, 2023-
Map releaseApr 12, 2023-
UpdateMay 13, 2026-
Current statusMay 13, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_26546.png

Downloads & links

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Map

FileDownload / File: emd_26546.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM of self-assembled cannula CanA
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 448 pix.
= 483.84 Å		1.08 Å/pix.
x 448 pix.
= 483.84 Å		1.08 Å/pix.
x 448 pix.
= 483.84 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.4
Minimum - Maximum-0.7709993 - 1.440544
Average (Standard dev.)0.0069667813 (±0.07911987)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-224-224-224
Dimensions448448448
Spacing448448448
CellA=B=C: 483.84003 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: half-map A

Fileemd_26546_half_map_1.map
Annotationhalf-map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half-map B

Fileemd_26546_half_map_2.map
Annotationhalf-map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : CanA

EntireName: CanA
Components
  • Complex: CanA
    • Protein or peptide: CanA
  • Ligand: CALCIUM ION
  • Ligand: water

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Supramolecule #1: CanA

SupramoleculeName: CanA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Pyrodictium abyssi (archaea)

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Macromolecule #1: CanA

MacromoleculeName: CanA / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pyrodictium abyssi (archaea)
Molecular weightTheoretical: 19.989492 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MTTQSPLNSF YATGTAQAVS EPIDVESHLG SITPAAGAQG SDDIGYAIVW IKDQVNDVKL KVTLANAEQL KPYFKYLQIQ ITSGYETNS TALGNFSETK AVISLDNPSA VIVLDKEDIA VLYPDKTGYT NTSIWVPGEP DKIIVYNETK PVAILNFKAF Y EAKEGMLF DSLPVIFNFQ VLQVG

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Macromolecule #2: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Macromolecule #3: water

MacromoleculeName: water / type: ligand / ID: 3 / Number of copies: 2 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 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: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 1.59 Å
Applied symmetry - Helical parameters - Δ&Phi: -173.747 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 659059
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE

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