+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-30672 | |||||||||
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Title | intermediate state of class C GPCR | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / G protein-coupled receptor dimeric complex / G protein-coupled receptor homodimeric complex / phospholipase C-activating G protein-coupled glutamate receptor signaling pathway / G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential / adenylate cyclase inhibiting G protein-coupled glutamate receptor activity / cellular response to electrical stimulus / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / regulation of sensory perception of pain / L-glutamate import across plasma membrane ...G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / G protein-coupled receptor dimeric complex / G protein-coupled receptor homodimeric complex / phospholipase C-activating G protein-coupled glutamate receptor signaling pathway / G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential / adenylate cyclase inhibiting G protein-coupled glutamate receptor activity / cellular response to electrical stimulus / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / regulation of sensory perception of pain / L-glutamate import across plasma membrane / G protein-coupled glutamate receptor signaling pathway / Class C/3 (Metabotropic glutamate/pheromone receptors) / glutamate receptor activity / Neurexins and neuroligins / regulation of synaptic transmission, glutamatergic / sensory perception of pain / locomotory behavior / G protein-coupled receptor activity / postsynaptic density membrane / Schaffer collateral - CA1 synapse / Sensory perception of sweet, bitter, and umami (glutamate) taste / chemical synaptic transmission / G alpha (q) signalling events / positive regulation of MAPK cascade / G protein-coupled receptor signaling pathway / glutamatergic synapse / dendrite / nucleus / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) / Lama glama (llama) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.65 Å | |||||||||
Authors | Zhang JY / Wu LJ / Luo F / Hua T / Liu ZJ | |||||||||
Citation | Journal: Protein Cell / Year: 2021 Title: Structural insights into the activation initiation of full-length mGlu1. Authors: Jinyi Zhang / Lu Qu / Lijie Wu / Xiaomeng Tang / Feng Luo / Weixiu Xu / Yueming Xu / Zhi-Jie Liu / Tian Hua / | |||||||||
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_30672.map.gz | 6.8 MB | EMDB map data format | |
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Header (meta data) | emd-30672-v30.xml emd-30672.xml | 10.9 KB 10.9 KB | Display Display | EMDB header |
Images | emd_30672.png | 105.3 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30672 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30672 | HTTPS FTP |
-Validation report
Summary document | emd_30672_validation.pdf.gz | 324 KB | Display | EMDB validaton report |
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Full document | emd_30672_full_validation.pdf.gz | 323.5 KB | Display | |
Data in XML | emd_30672_validation.xml.gz | 6.2 KB | Display | |
Data in CIF | emd_30672_validation.cif.gz | 7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30672 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30672 | HTTPS FTP |
-Related structure data
Related structure data | 7dgeMC 7dgdC 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_30672.map.gz / Format: CCP4 / Size: 91.1 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: 1.04 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 : dimer of intermediate state
Entire | Name: dimer of intermediate state |
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Components |
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-Supramolecule #1: dimer of intermediate state
Supramolecule | Name: dimer of intermediate state / type: cell / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Metabotropic glutamate receptor 1
Macromolecule | Name: Metabotropic glutamate receptor 1 / 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: 93.398867 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: GASSQRSVAR MDGDVIIGAL FSVHHQPPAE KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQS IEFIRDSLIS IRDEKDGINR CLPDGQSLPP GRTKKPIAGV IGPGSSSVAI QVQNLLQLFD IPQIAYSATS I DLSDKTLY ...String: GASSQRSVAR MDGDVIIGAL FSVHHQPPAE KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQS IEFIRDSLIS IRDEKDGINR CLPDGQSLPP GRTKKPIAGV IGPGSSSVAI QVQNLLQLFD IPQIAYSATS I DLSDKTLY KYFLRVVPSD TLQARAMLDI VKRYNWTYVS AVHTEGNYGE SGMDAFKELA AQEGLCIAHS DKIYSNAGEK SF DRLLRKL RERLPKARVV VCFCEGMTVR GLLSAMRRLG VVGEFSLIGS DGWADRDEVI EGYEVEANGG ITIKLQSPEV RSF DDYFLK LRLDTNHRNP WFQEFWQHRF QCRLEGFPQE NSNFKRICTG NESLEENYVQ DSKMGFVINA IYAMAHGLQN MHHA LCPGH VGLCDAMKPI DGSKLLDFLI KSSFIGVSGE EVWFDEKGDA PGRYDIMNLQ YTEANRYDYV HVGTWHEGVL NIDDY KIQM NKSGVVRSVC SEPCLKGQIK VIRKGEVSCC WICTACKENE YVQDEFTCKA CDLGWWPNAD LTGCEPIPVR YLEWSN IES IIAIAFSCLG ILVTLFVTLI FVLYRDTPVV KSSSRELCYI ILAGIFLGYV CPFTLIAKPT TTSCYLQRLL VGLSSAM CY SALVTKTNRI ARILAGSKKK ICTRKPRFMS AWAQVIIASI LISVQLTLVV TLIIMEPPMP ILSYPSIKEV YLICNTSN L GVVAPLGYNG LLIMSCTYYA FKTRNVPANF NEAKYIAFTM YTTCIIWLAF VPIYFGSNYK IITTCFAVSL SVTVALGCM FTPKMYIIIA KPERNVRSAF TTSDVVRMHV GDG |
-Macromolecule #2: nanobody
Macromolecule | Name: nanobody / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Lama glama (llama) |
Molecular weight | Theoretical: 13.354672 KDa |
Recombinant expression | Organism: Escherichia coli BL21(DE3) (bacteria) |
Sequence | String: QVQLVESGGG LVQAGGSLRL SCAASGRTFT SYAMGWFRQA PGKERESVAA ISSSGGSTHY ADSVKGRFTI SRDNSKNTVY LQMNSLKPE DTAVYYCAAA MYGSRWPDWE YDYWGQGTQV TVSS |
-Macromolecule #3: (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID
Macromolecule | Name: (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID type: ligand / ID: 3 / Number of copies: 1 / Formula: QUS |
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Molecular weight | Theoretical: 189.126 Da |
Chemical component information | ChemComp-QUS: |
-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 TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 1.33 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.65 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 58627 |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |