9ifo

Structure of Teneurin-Like Protein (TLP)

spinqualitylabelsall models 9ifo, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ifo is a 2 chain structure with sequence from Bacillus subtilis group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Ancestral neuronal receptors are bacterial accessory toxins.,Raoelijaona F, Szczepaniak J, Schahl A, Bray JE, Zhou JC, Baker L, El Omari K, Lowe E, Low YS, Rodriguez CM, Landsberg MJ, Lott JS, Kleanthous C, Chavent M, Maiden MC, Seiradake E Nat Commun. 2026 Feb 14. doi: 10.1038/s41467-026-69246-x. PMID:41690916 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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