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- EMDB-52847: Structure of Teneurin-Like Protein (TLP) -

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Basic information

Entry
Database: EMDB / ID: EMD-52847
TitleStructure of Teneurin-Like Protein (TLP)
Map data
Sample
  • Organelle or cellular component: Teneurin-like protein
    • Protein or peptide: Teneurin-Like Protein
  • Protein or peptide: Teneurin-Like Protein
KeywordsRHS/YD-repeat protein / Toxin / CELL ADHESION
Biological speciesBacillus inaquosorum (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.1 Å
AuthorsRaoelijaona F / Zhou J / El-Omari K / Lowe ED / Seiradake E
Funding support United Kingdom, 2 items
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, 2025-
Header (metadata) releaseMar 11, 2026-
Map releaseMar 11, 2026-
UpdateMar 11, 2026-
Current statusMar 11, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_52847.png

Downloads & links

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Map

FileDownload / File: emd_52847.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 320 pix.
= 266.24 Å		0.83 Å/pix.
x 320 pix.
= 266.24 Å		0.83 Å/pix.
x 320 pix.
= 266.24 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.832 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.256
Minimum - Maximum-1.5899602 - 3.7847593
Average (Standard dev.)0.0002131175 (±0.077024825)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 266.24 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_52847_additional_1.map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_52847_half_map_1.map
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_52847_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Teneurin-like protein

EntireName: Teneurin-like protein
Components
  • Organelle or cellular component: Teneurin-like protein
    • Protein or peptide: Teneurin-Like Protein
  • Protein or peptide: Teneurin-Like Protein

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Supramolecule #1: Teneurin-like protein

SupramoleculeName: Teneurin-like protein / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1 / Details: Monomeric structure of teneurin-like protein
Source (natural)Organism: Bacillus inaquosorum (bacteria)
Molecular weightTheoretical: 184 KDa

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Macromolecule #1: Teneurin-Like Protein

MacromoleculeName: Teneurin-Like Protein / type: protein_or_peptide / ID: 1
Details: A2144/A2145 break - result of autoproteolytic cleavage
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bacillus inaquosorum (bacteria)
Molecular weightTheoretical: 229.323328 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MEERPSPPHL VALTIIPASI VLDVGETHQF QVMGNFSDGS SKDLTKRARY KSSNSNIVKV NNSSHNKGLA TAITAGESEI TARVRQFKV VANIRVQAAV NLTGITIEPT SVILPVGNTQ QFTVTGQFSD GSTQDLTDQA SYLSSSTNVV TVYNNGLATA V SSGTAQIT ...String:
MEERPSPPHL VALTIIPASI VLDVGETHQF QVMGNFSDGS SKDLTKRARY KSSNSNIVKV NNSSHNKGLA TAITAGESEI TARVRQFKV VANIRVQAAV NLTGITIEPT SVILPVGNTQ QFTVTGQFSD GSTQDLTDQA SYLSSSTNVV TVYNNGLATA V SSGTAQIT AAVNGFTAIA SLEVQAAVTL TGITIEPTSV ILPAGNTQQF TVTGQFSDGS TQDLTDQASY LSSNTNVVTV DN NGLATAV SSGTAQITAA VNSFTAIASL EVQAAVTLIG ITIEPTSVVL KVEETQQFTV TGRFSDGSTQ DVTEQASYAS SNP NVVTIA NTGLATAVAL GSATITATAD GFTAIATLNV HTIVVPPLDM SGATSVFSSS AFLYTGENPI QTGVQPGTIE LRRA AVLRG QVFNRDGEPL SRVNISILDH PEFGSTFTRE DGQFDMAVNG GELLIVRYEK NGLRPVQRRI EVPWEDFVIL PDVQM IALD PVVTTIDLSQ PDIQTARGSE ILDVEGTRQA TLLFPPGNKA TMILPDGTTQ EISTLNVRAT EYSVGEGGPN AMPALL PPT SAYTYCVEFS ADEELAAGAR EVRFDQPIVF YVENFLEFPV GGAVPTGFYD RIQGEWIASR NGQVIQIVSI TGGLADL DI DGDGAADSAD DLAELGITNA ERQRLANLYQ TGQSLWRVPI THFSAPWDCN WPYGFPDDSD RPRNPDPFDK PKPDDDCN K EGSIIGALAQ TLGEEVQVTG TPFRMHYHSD RVRGRKEAYS LEIPLSGTNI PQSVQRIRLD IFVAGRCITE SFPPATNLT HTFVWDGKDA YGRVLQGSHP ITVRIRYEYQ LVYLTPAAFR TSFGRITGEG GGSGGGGAGT PLIIARRGDP NASLTQEFKG SIGLFDTRE QGLGAWTLSV HHFYDPISRV LFLGDGQRRS AESLSTVIAT VAGTNYGFSG DGGPATQAQL RAPRDMAVGS D GSLYIADT ENERIRRVGP DGIITTVAGT GVQGFSGDGG PATQAQLGSP RGVAVGSDGS LYIVDAGNVR IRRVGPDGII TT VAGTGVS GFSGDGGPAT QAQLSFPPGG VAVGSDGSLF IADTLNNRIR RVGPDGIITT VAGTGDFGFS GDGGPAAQAT LRI PGDVSV GSDGSLYIAD SQNVRIRRVG PDGIINTVAG TGVQGFSGDG GPATQAQLRL PRGVDVGSDG YLYIVDESRT RRVR DGIIT TVVGTGVQGF SGDGGPATQA TLWVPADVAV GSDGSLFIAD TGNNRIRRVA SVLPGTTRTD ILIPSADGSE VVIFN ESGK HLRTLDALTG AIRFRFIYNN DGHLVQVQDV DGNSTIIERD STGNPISIVA PGGQRTALTL DANGFLASIT NPAREA FQF EYNPDGLMTS QIDPRGNISR FEYDSGGHLI RDEHPTGGVT TLMRTNSTNG FVVTLTSPLG RVSTFQLERL TTGTLKQ VV IDSNGGRTES LTGTDGKQQI TYPDGTQLVD QVGPDPRFGM LAHIVRRRTV TTPGGLSFLH VTDRQAVLSD PTNLLSLQ K LTTTVSINDR IFRTIFDAGT RETTITTPVG RKSVIGFDSI GRVNRQILAT GVDPILFTYN NQGQLTERQQ GNVITNLIY DSLLRLQAIV DNAGRESRFS YDNADRVIQI TRCGGDIERL TYDSNGNPTQ VIRPNGSVHT LSYTPVNLLG GYTPPGNPGY TFLYNVERQ IRRKILPTGR TIDLTYDSGG RLTDVIYPEA AVTLVYTAGD PTQRVNRLLR TPIGGGPTQE MELTYDASLI T GMTFTGIS QGAFTYTYDS NFSLVNVGLV SGSDQVQVGI SRNADGLITG LGSFTITRSG PDGKISRISD GALNRTMSYD TI ARLSSYN DTVGGQQIYR SDFQYDNASR LQRKTETVGS AAHTLEYSYD TSCNLIEVTK DGMVVESYTY DANGNRTSRQ VMG GPVEMA TYDNQDRLVH RDGINYEFNA DGFMVSRGSD TFEYSALGEL LQATVGGKTI TYVYDGLGRR VSRTESTGTT QYLY GNPEN LLQVTAIRDP SGQLNMLFYD DNDFLFAFDR DGTKFYVTTD LVGTPRVVTN GTGTVLRELE HDSFGNIIAD SNPRF VLPI GFAGGLADPD TELVRFGYRD YEPASGRWTA QDPILFRSGD FNLYAYVHNN PVTLRDPSGL

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Macromolecule #2: Teneurin-Like Protein

MacromoleculeName: Teneurin-Like Protein / type: protein_or_peptide / ID: 2
Details: A2144/A2145 break - result of autoproteolytic cleavage
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bacillus inaquosorum (bacteria)
Molecular weightTheoretical: 6.647664 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
ICLSKADITT LKEINDVIKI VGGFLFANPY ATAAGIGISN SLIIDAIDEC PQEPPKPANK CPE

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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

BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 38.3 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 5851862
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.6.2) / Number images used: 3010268
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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