Journal: Nat Commun / Year: 2018 Title: Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction. Authors: Verity A Jackson / Dimphna H Meijer / Maria Carrasquero / Laura S van Bezouwen / Edward D Lowe / Colin Kleanthous / Bert J C Janssen / Elena Seiradake / Abstract: Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event ...Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.
History
Deposition
Dec 18, 2017
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Header (metadata) release
Mar 28, 2018
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Map release
Mar 28, 2018
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Update
Jul 29, 2020
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Current status
Jul 29, 2020
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Details: We have used PDB 6FB3 (same publication) as a template model using Modeller v9.16 followed by manual rebuilding in Coot and real-space refinement using Phenix.
Refinement
Space: REAL / Protocol: OTHER / Overall B value: 126
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