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- PDB-9ifo: Structure of Teneurin-Like Protein (TLP) -

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Basic information

Entry
Database: PDB / ID: 9ifo
TitleStructure of Teneurin-Like Protein (TLP)
Components(Teneurin-Like Protein) x 2
KeywordsCELL ADHESION / RHS/YD-repeat protein / Toxin
Biological speciesBacillus inaquosorum (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.1 Å
AuthorsRaoelijaona, F. / Zhou, J. / El-Omari, K. / Lowe, E.D. / Seiradake, E.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust202827/Z/16/Z United Kingdom
Wellcome Trust226647/Z/22/Z United Kingdom
CitationJournal: Nat Commun / Year: 2026
Title: Ancestral neuronal receptors are bacterial accessory toxins.
Authors: Finaritra Raoelijaona / Joanna Szczepaniak / Adrien Schahl / James E Bray / Jin Chuan Zhou / Lindsay Baker / Kamel El Omari / Edward Lowe / Yu Shang Low / Chandra M Rodriguez / Michael J ...Authors: Finaritra Raoelijaona / Joanna Szczepaniak / Adrien Schahl / James E Bray / Jin Chuan Zhou / Lindsay Baker / Kamel El Omari / Edward Lowe / Yu Shang Low / Chandra M Rodriguez / Michael J Landsberg / J Shaun Lott / Colin Kleanthous / Matthieu Chavent / Martin Cj Maiden / Elena Seiradake /
Abstract: Horizontal gene transfer events were crucial in the emergence of multicellular life. A striking example is the acquisition of Teneurins, putative surface-exposed toxins in bacteria that function as ...Horizontal gene transfer events were crucial in the emergence of multicellular life. A striking example is the acquisition of Teneurins, putative surface-exposed toxins in bacteria that function as cell adhesion receptors in metazoan neuronal development. Here, we demonstrate the evolutionary relationships between metazoan and bacterial Teneurins. We use cryogenic electron microscopy and bioinformatic analysis to show that bacterial Teneurins harbour a toxic protein in a proteinaceous shell. They are rare but widely distributed across bacterial taxa and are predominantly seen in species with complex social behaviours, suggesting roles in cell-to-cell interaction. This work confirms that metazoan Teneurins are repurposed bacterial toxins that have evolved to be essential mediators of intercellular communication in all advanced nervous systems. Their acquisition was a key event in the evolution of metazoans.
History
DepositionFeb 18, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 11, 2026Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Teneurin-Like Protein
B: Teneurin-Like Protein


Theoretical massNumber of molelcules
Total (without water)235,9712
Polymers235,9712
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Teneurin-Like Protein


Mass: 229323.328 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: A2144/A2145 break - result of autoproteolytic cleavage
Source: (gene. exp.) Bacillus inaquosorum (bacteria) / Production host: Escherichia coli (E. coli)
#2: Protein Teneurin-Like Protein


Mass: 6647.664 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: A2144/A2145 break - result of autoproteolytic cleavage
Source: (gene. exp.) Bacillus inaquosorum (bacteria) / Production host: Escherichia coli (E. coli)
Has protein modificationY

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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: Teneurin-like protein / Type: ORGANELLE OR CELLULAR COMPONENT / Details: Monomeric structure of teneurin-like protein / Entity ID: #1 / Source: RECOMBINANT
Molecular weightValue: 0.184 MDa / Experimental value: NO
Source (natural)Organism: Bacillus inaquosorum (bacteria)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen 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: 2200 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 38.3 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1PHENIX1.21rc1_5109model refinement
3SIMPLE3particle selection
7cryoSPARC4.6.23D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 5851862
3D reconstructionResolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 3010268 / Symmetry type: POINT
RefinementCross valid method: NONE

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