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- EMDB-71831: Bacillus subtilis teneurin-like protein -

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Basic information

Entry
Database: EMDB / ID: EMD-71831
TitleBacillus subtilis teneurin-like protein
Map data
Sample
  • Complex: Bacillus subtilis teneurin-like protein
    • Protein or peptide: Teneurin-like protein
Keywordsbacterial toxins / TOXIN
Biological speciesBacillus subtilis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.74 Å
AuthorsLow YS / Landsberg MJL
Funding support Australia, New Zealand, 3 items
OrganizationGrant numberCountry
Australian Research Council (ARC)DP220101681 Australia
Australian Research Council (ARC)DP170104484 Australia
Marsden Fund New Zealand
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
DepositionJul 27, 2025-
Header (metadata) releaseMay 6, 2026-
Map releaseMay 6, 2026-
UpdateMay 6, 2026-
Current statusMay 6, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_71831.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.14 Å/pix.
x 256 pix.
= 291.84 Å
1.14 Å/pix.
x 256 pix.
= 291.84 Å
1.14 Å/pix.
x 256 pix.
= 291.84 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.14 Å
Density
Contour LevelBy AUTHOR: 0.0577
Minimum - Maximum-0.011726621 - 1.6496865
Average (Standard dev.)0.0009439605 (±0.019209435)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 291.84 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_71831_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_71831_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_71831_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Bacillus subtilis teneurin-like protein

EntireName: Bacillus subtilis teneurin-like protein
Components
  • Complex: Bacillus subtilis teneurin-like protein
    • Protein or peptide: Teneurin-like protein

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Supramolecule #1: Bacillus subtilis teneurin-like protein

SupramoleculeName: Bacillus subtilis teneurin-like protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Bacillus subtilis (bacteria)
Molecular weightTheoretical: 240 KDa

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Macromolecule #1: Teneurin-like protein

MacromoleculeName: Teneurin-like protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bacillus subtilis (bacteria)
Molecular weightTheoretical: 239.074734 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 ICLSKADITT LKEIND VIK IVGAVATAGG FLFANPYATA AGIGISLGGA INSLIIDAID ECPQEPPKPA NKCPERQPVN FKRDSPEPTI IELD

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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

Concentration0.8 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeJEOL CRYO ARM 300
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 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

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Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: Ab initio map
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.74 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 119873
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT / Overall B value: 121.8
Output model

PDB-9pt5:
Bacillus subtilis teneurin-like protein

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