+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-31237 | |||||||||||||||
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Title | Cryo-EM structure of inactive mGlu7 homodimer | |||||||||||||||
Map data | ||||||||||||||||
Sample |
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Function / homology | Function and homology information group III metabotropic glutamate receptor activity / adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway / adenylate cyclase inhibitor activity / negative regulation of glutamate secretion / adenylate cyclase inhibiting G protein-coupled glutamate receptor activity / serine binding / plasma membrane => GO:0005886 / G protein-coupled glutamate receptor signaling pathway / Class C/3 (Metabotropic glutamate/pheromone receptors) / glutamate receptor activity ...group III metabotropic glutamate receptor activity / adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway / adenylate cyclase inhibitor activity / negative regulation of glutamate secretion / adenylate cyclase inhibiting G protein-coupled glutamate receptor activity / serine binding / plasma membrane => GO:0005886 / G protein-coupled glutamate receptor signaling pathway / Class C/3 (Metabotropic glutamate/pheromone receptors) / glutamate receptor activity / glutamate binding / presynaptic active zone / asymmetric synapse / regulation of synaptic transmission, glutamatergic / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / dendritic shaft / PDZ domain binding / membrane => GO:0016020 / sensory perception of sound / cell cortex / G alpha (i) signalling events / chemical synaptic transmission / postsynaptic membrane / receptor complex / G protein-coupled receptor signaling pathway / axon / dendrite / calcium ion binding / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | |||||||||||||||
Authors | Du J / Wang D / Fan H / Tai L / Lin S / Han S / Sun F / Wu B / Zhao Q | |||||||||||||||
Funding support | China, 4 items
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Citation | Journal: Nature / Year: 2021 Title: Structures of human mGlu2 and mGlu7 homo- and heterodimers. Authors: Juan Du / Dejian Wang / Hongcheng Fan / Chanjuan Xu / Linhua Tai / Shuling Lin / Shuo Han / Qiuxiang Tan / Xinwei Wang / Tuo Xu / Hui Zhang / Xiaojing Chu / Cuiying Yi / Peng Liu / Xiaomei ...Authors: Juan Du / Dejian Wang / Hongcheng Fan / Chanjuan Xu / Linhua Tai / Shuling Lin / Shuo Han / Qiuxiang Tan / Xinwei Wang / Tuo Xu / Hui Zhang / Xiaojing Chu / Cuiying Yi / Peng Liu / Xiaomei Wang / Yu Zhou / Jean-Philippe Pin / Philippe Rondard / Hong Liu / Jianfeng Liu / Fei Sun / Beili Wu / Qiang Zhao / Abstract: The metabotropic glutamate receptors (mGlus) are involved in the modulation of synaptic transmission and neuronal excitability in the central nervous system. These receptors probably exist as both ...The metabotropic glutamate receptors (mGlus) are involved in the modulation of synaptic transmission and neuronal excitability in the central nervous system. These receptors probably exist as both homo- and heterodimers that have unique pharmacological and functional properties. Here we report four cryo-electron microscopy structures of the human mGlu subtypes mGlu2 and mGlu7, including inactive mGlu2 and mGlu7 homodimers; mGlu2 homodimer bound to an agonist and a positive allosteric modulator; and inactive mGlu2-mGlu7 heterodimer. We observed a subtype-dependent dimerization mode for these mGlus, as a unique dimer interface that is mediated by helix IV (and that is important for limiting receptor activity) exists only in the inactive mGlu2 structure. The structures provide molecular details of the inter- and intra-subunit conformational changes that are required for receptor activation, which distinguish class C G-protein-coupled receptors from those in classes A and B. Furthermore, our structure and functional studies of the mGlu2-mGlu7 heterodimer suggest that the mGlu7 subunit has a dominant role in controlling dimeric association and G-protein activation in the heterodimer. These insights into mGlu homo- and heterodimers highlight the complex landscape of mGlu dimerization and activation. | |||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_31237.map.gz | 147.1 MB | EMDB map data format | |
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Header (meta data) | emd-31237-v30.xml emd-31237.xml | 11.5 KB 11.5 KB | Display Display | EMDB header |
Images | emd_31237.png | 101.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-31237 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-31237 | HTTPS FTP |
-Validation report
Summary document | emd_31237_validation.pdf.gz | 435.1 KB | Display | EMDB validaton report |
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Full document | emd_31237_full_validation.pdf.gz | 434.7 KB | Display | |
Data in XML | emd_31237_validation.xml.gz | 6.7 KB | Display | |
Data in CIF | emd_31237_validation.cif.gz | 7.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31237 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-31237 | HTTPS FTP |
-Related structure data
Related structure data | 7epcMC 7epaC 7epbC 7epdC 7epeC 7epfC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_31237.map.gz / Format: CCP4 / Size: 181 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Inactive mGlu7 homodimer
Entire | Name: Inactive mGlu7 homodimer |
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Components |
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-Supramolecule #1: Inactive mGlu7 homodimer
Supramolecule | Name: Inactive mGlu7 homodimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: mammal environmental sample (environmental samples) |
-Macromolecule #1: Isoform 3 of Metabotropic glutamate receptor 7
Macromolecule | Name: Isoform 3 of Metabotropic glutamate receptor 7 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 96.276977 KDa |
Recombinant expression | Organism: mammal environmental sample (environmental samples) |
Sequence | String: GAPQEMYAPH SIRIEGDVTL GGLFPVHAKG PSGVPCGDIK RENGIHRLEA MLYALDQINS DPNLLPNVTL GARILDTCSR DTYALEQSL TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA STAPELSDDR R YDFFSRVV ...String: GAPQEMYAPH SIRIEGDVTL GGLFPVHAKG PSGVPCGDIK RENGIHRLEA MLYALDQINS DPNLLPNVTL GARILDTCSR DTYALEQSL TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA STAPELSDDR R YDFFSRVV PPDSFQAQAM VDIVKALGWN YVSTLASEGS YGEKGVESFT QISKEAGGLC IAQSVRIPQE RKDRTIDFDR II KQLLDTP NSRAVVIFAN DEDIKQILAA AKRADQVGHF LWVGSDSWGS KINPLHQHED IAEGAITIQP KRATVEGFDA YFT SRTLEN NRRNVWFAEY WEENFNCKLT ISGSKKEDTD RKCTGQERIG KDSNYEQEGK VQFVIDAVYA MAHALHHMNK DLCA DYRGV CPEMEQAGGK KLLKYIRNVN FNGSAGTPVM FNKNGDAPGR YDIFQYQTTN TSNPGYRLIG QWTDELQLNI EDMQW GKGV REIPASVCTL PCKPGQRKKT QKGTPCCWTC EPCDGYQYQF DEMTCQHCPY DQRPNENRTG CQDIPIIKLE WHSPWA VIP VFLAMLGIIA TIFVMATFIR YNDTPIVRAS GRELSYVLLT GIFLCYIITF LMIAKPDVAV CSFRRVFLGL GMCISYA AL LTKTYRIYRI FEQGKKSVTA PRLISPTSQL AITSSLISVQ LLGVFIWFIV DPPNIIIDYD EHKTMNPEQA RGVLKCDI T DLQIICSLGY SILLMVTCTV YAFKTRGVPE NFNEAKYIGF TMYTTCIVWL AFIPIFFGTA QSAEKLYIQT TTLTISMNL SASVALGMLY MPKVYIIIFH PELNVQKREF LEVLFQGPGS GSWSHPQFEK DYKDDDD |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 1.47 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1011214 |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |