+Open data
-Basic information
Entry | Database: PDB / ID: 7plp | ||||||
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Title | Human Teneurin-4 C-rich domain | ||||||
Components | Teneurin-4 | ||||||
Keywords | CELL ADHESION / cysteine-rich / calcium binding | ||||||
Function / homology | Function and homology information cardiac cell fate specification / positive regulation of myelination / central nervous system myelin formation / positive regulation of gastrulation / gastrulation with mouth forming second / cardiac muscle cell proliferation / regulation of myelination / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / positive regulation of oligodendrocyte differentiation / neuron development ...cardiac cell fate specification / positive regulation of myelination / central nervous system myelin formation / positive regulation of gastrulation / gastrulation with mouth forming second / cardiac muscle cell proliferation / regulation of myelination / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / positive regulation of oligodendrocyte differentiation / neuron development / cell adhesion molecule binding / neuron projection / protein heterodimerization activity / signal transduction / protein homodimerization activity / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.4 Å | ||||||
Authors | Beugelink, J.W. / Meijer, D.H. / Janssen, B.J.C. | ||||||
Funding support | Netherlands, 1items
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Citation | Journal: EMBO J / Year: 2022 Title: Teneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions. Authors: Dimphna H Meijer / Cátia P Frias / J Wouter Beugelink / Yanthi N Deurloo / Bert J C Janssen / Abstract: Establishment of correct synaptic connections is a crucial step during neural circuitry formation. The Teneurin family of neuronal transmembrane proteins promotes cell-cell adhesion via homophilic ...Establishment of correct synaptic connections is a crucial step during neural circuitry formation. The Teneurin family of neuronal transmembrane proteins promotes cell-cell adhesion via homophilic and heterophilic interactions, and is required for synaptic partner matching in the visual and hippocampal systems in vertebrates. It remains unclear how individual Teneurins form macromolecular cis- and trans-synaptic protein complexes. Here, we present a 2.7 Å cryo-EM structure of the dimeric ectodomain of human Teneurin4. The structure reveals a compact conformation of the dimer, stabilized by interactions mediated by the C-rich, YD-shell, and ABD domains. A 1.5 Å crystal structure of the C-rich domain shows three conserved calcium binding sites, and thermal unfolding assays and SAXS-based rigid-body modeling demonstrate that the compactness and stability of Teneurin4 dimers are calcium-dependent. Teneurin4 dimers form a more extended conformation in conditions that lack calcium. Cellular assays reveal that the compact cis-dimer is compatible with homomeric trans-interactions. Together, these findings support a role for teneurins as a scaffold for macromolecular complex assembly and the establishment of cis- and trans-synaptic interactions to construct functional neuronal circuits. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7plp.cif.gz | 50.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7plp.ent.gz | 35.7 KB | Display | PDB format |
PDBx/mmJSON format | 7plp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pl/7plp ftp://data.pdbj.org/pub/pdb/validation_reports/pl/7plp | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein/peptide , 1 types, 2 molecules AB
#1: Protein/peptide | Mass: 5200.784 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TENM4, KIAA1302, ODZ4, TNM4 / Cell line (production host): HEK cells / Production host: Homo sapiens (human) / References: UniProt: Q6N022 |
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-Non-polymers , 5 types, 67 molecules
#2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-FE / | #4: Chemical | ChemComp-SO4 / | #5: Chemical | ChemComp-NI / | #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.42 % |
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Crystal grow | Temperature: 293 K / Method: batch mode / pH: 7.5 Details: 0.085 M HEPES pH 7.5, 1.7 v/v % PEG-400, 1.7 M (NH4)2SO4, 15 w/v % glycerol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.7749 Å | ||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 26, 2021 | ||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.7749 Å / Relative weight: 1 | ||||||||||||||||||||||||
Reflection | Resolution: 1.4→46.91 Å / Num. obs: 19462 / % possible obs: 100 % / Redundancy: 41.2 % / CC1/2: 0.999 / Rmerge(I) obs: 0.184 / Rpim(I) all: 0.029 / Rrim(I) all: 0.186 / Net I/σ(I): 14 / Num. measured all: 802023 / Scaling rejects: 715 | ||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: From unpublished anomalous experiment Resolution: 1.4→33.19 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.976 / SU B: 1.96 / SU ML: 0.032 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.054 / ESU R Free: 0.048 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 129.83 Å2 / Biso mean: 23.684 Å2 / Biso min: 12 Å2
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Refinement step | Cycle: final / Resolution: 1.4→33.19 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.4→1.437 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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