9IFO
Structure of Teneurin-Like Protein (TLP)
Summary for 9IFO
| Entry DOI | 10.2210/pdb9ifo/pdb |
| EMDB information | 52847 |
| Descriptor | Teneurin-Like Protein (2 entities in total) |
| Functional Keywords | rhs/yd-repeat protein, toxin, cell adhesion |
| Biological source | Bacillus inaquosorum More |
| Total number of polymer chains | 2 |
| Total formula weight | 235970.99 |
| Authors | Raoelijaona, F.,Zhou, J.,El-Omari, K.,Lowe, E.D.,Seiradake, E. (deposition date: 2025-02-18, release date: 2026-03-11) |
| Primary citation | Raoelijaona, F.,Szczepaniak, J.,Schahl, A.,Bray, J.E.,Zhou, J.C.,Baker, L.,El Omari, K.,Lowe, E.,Low, Y.S.,Rodriguez, C.M.,Landsberg, M.J.,Lott, J.S.,Kleanthous, C.,Chavent, M.,Maiden, M.C.,Seiradake, E. Ancestral neuronal receptors are bacterial accessory toxins. Nat Commun, 2026 Cited by PubMed 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 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. PubMed: 41690916DOI: 10.1038/s41467-026-69246-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.1 Å) |
Structure validation
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