[English] 日本語
Yorodumi
- PDB-6n52: Metabotropic Glutamate Receptor 5 Apo Form -

+
Open data


ID or keywords:

Loading...

no data

-
Basic information

Entry
Database: PDB / ID: 6n52
TitleMetabotropic Glutamate Receptor 5 Apo Form
ComponentsMetabotropic glutamate receptor 5
KeywordsMEMBRANE PROTEIN / Cell Surface Receptor
Function / homologyGPCR, family 3, conserved site / Homer-binding domain of metabotropic glutamate receptor / Periplasmic binding protein-like I / Metabotropic glutamate receptor, Homer-binding domain / GPCR, family 3, metabotropic glutamate receptor / Receptor family ligand binding region / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, metabotropic glutamate receptor 5 / GPCR, family 3 / Receptor, ligand binding region ...GPCR, family 3, conserved site / Homer-binding domain of metabotropic glutamate receptor / Periplasmic binding protein-like I / Metabotropic glutamate receptor, Homer-binding domain / GPCR, family 3, metabotropic glutamate receptor / Receptor family ligand binding region / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, metabotropic glutamate receptor 5 / GPCR, family 3 / Receptor, ligand binding region / GPCR, family 3, nine cysteines domain / G-protein coupled receptors family 3 signature 1. / GPCR, family 3, nine cysteines domain superfamily / G-protein coupled receptors family 3 signature 2. / GPCR family 3, C-terminal / G-protein coupled receptors family 3 signature 3. / G-protein coupled receptors family 3 profile. / G alpha (q) signalling events / Class C/3 (Metabotropic glutamate/pheromone receptors) / Neurexins and neuroligins / 7 transmembrane sweet-taste receptor of 3 GCPR / regulation of translational elongation / phospholipase C-activating G protein-coupled glutamate receptor signaling pathway / G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential / trans-synaptic signaling by endocannabinoid, modulating synaptic transmission / protein tyrosine kinase activator activity / postsynaptic modulation of chemical synaptic transmission / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / G protein-coupled glutamate receptor signaling pathway / regulation of intracellular calcium activated chloride channel activity / glutamate receptor activity / postsynaptic density membrane / G protein-coupled receptor activity / modulation of age-related behavioral decline / calcium-mediated signaling using intracellular calcium source / synapse organization / protein tyrosine kinase binding / regulation of synaptic transmission, glutamatergic / locomotory behavior / cognition / regulation of protein phosphorylation / learning / regulation of long-term neuronal synaptic plasticity / positive regulation of protein tyrosine kinase activity / Schaffer collateral - CA1 synapse / learning or memory / cellular response to amyloid-beta / regulation of translation / chemical synaptic transmission / neuron projection / G protein-coupled receptor signaling pathway / integral component of plasma membrane / plasma membrane / cytoplasm / Metabotropic glutamate receptor 5
Function and homology information
Specimen sourceHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 4 Å resolution
AuthorsKoehl, A. / Hu, H. / Feng, D. / Sun, B. / Weis, W.I. / Skiniotis, G.S. / Mathiesen, J.M. / Kobilka, B.K.
CitationJournal: Nature / Year: 2019
Title: Structural insights into the activation of metabotropic glutamate receptors.
Authors: Antoine Koehl / Hongli Hu / Dan Feng / Bingfa Sun / Yan Zhang / Michael J Robertson / Matthew Chu / Tong Sun Kobilka / Toon Laermans / Jan Steyaert / Jeffrey Tarrasch / Somnath Dutta / Rasmus Fonseca / William I Weis / Jesper M Mathiesen / Georgios Skiniotis / Brian K Kobilka
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Nov 20, 2018 / Release: Jan 23, 2019
RevisionDateData content typeGroupCategoryItemProviderType
1.0Jan 23, 2019Structure modelrepositoryInitial release
1.1Feb 6, 2019Structure modelData collection / Database referencescitation / citation_author_citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.name

-
Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
  • Download
  • Superimposition on EM map
  • EMDB-0346
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Metabotropic glutamate receptor 5
B: Metabotropic glutamate receptor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)196,2416
Polyers195,3562
Non-polymers8854
Water0
1


  • idetical with deposited unit
  • defined by author
  • Evidence: gel filtration, Single peak that confirmed presence of mGlu5 by SDS PAGE
  • Download structure data
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area (Å2)2140
ΔGint (kcal/M)-2
Surface area (Å2)75220

-
Components

#1: Protein/peptide Metabotropic glutamate receptor 5 / / mGluR5


Mass: 97677.945 Da / Num. of mol.: 2 / Source: (gene. exp.) Homo sapiens (human) / Gene: GRM5, GPRC1E, MGLUR5 / Plasmid name: PVL1392 / Cell line (production host): SF9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P41594
#2: Chemical
ChemComp-NAG / N-ACETYL-D-GLUCOSAMINE


Mass: 221.208 Da / Num. of mol.: 4 / Formula: C8H15NO6 / N-Acetylglucosamine

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / Reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: Metabotropic Glutamate Receptor 5 in Nanodiscs / Type: COMPLEX / Details: Metabotropic Glutamate Receptor 5 in Nanodiscs / Entity ID: 1 / Source: RECOMBINANT
Molecular weightValue: 0.2 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm) / Strain: Sf9
Buffer solutionDetails: 100mM NaCl, 20 mM HEPES pH 7.5, 5uM FFMTEB added as a negative allosteric modulator.
pH: 7.5
Buffer component
IDConc.NameFormulaBuffer ID
1100 mMsodium chlorideNaCl1
220 mMHEPESHEPES1
SpecimenConc.: 7 mg/ml
Details: This sample was mono disperse as assayed by gel filtration.
Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 200 / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 293 kelvins
Details: Addition 0.0005% Amphipol A8-35was added to sample prior to apply to grid; 3.5ul sample was applied; blot for 1s before plunging

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 130000 / Calibrated magnification: 47169 / Cs: 2.7 mm / C2 aperture diameter: 50 microns
Image recordingElectron dose: 50 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

-
Processing

EM software
IDNameVersionCategory
2SerialEMimage acquisition
11RELION2.1final Euler assignment
12RELION2.1classification
13RELION3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 123096 / Symmetry type: POINT

+
About Yorodumi

-
News

-
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force. (see PDBe EMDB page)
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.: Q: What is "EMD"? / ID/Accession-code notation in Yorodumi/EM Navigator

External links: EMDB at EBI / Contact to PDBj

-
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary. This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated. See below links for details.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software). Now, EM Navigator and Yorodumi are based on the updated data.

External links: wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

+
Jun 16, 2017. Omokage search with filter

Omokage search with filter

  • Result of Omokage search can be filtered by keywords and the database types

Related info.: Omokage search

+
Sep 15, 2016. EM Navigator & Yorodumi renewed

EM Navigator & Yorodumi renewed

  • New versions of EM Navigator and Yorodumi started

Related info.: Changes in new EM Navigator and Yorodumi

+
Aug 31, 2016. New EM Navigator & Yorodumi

New EM Navigator & Yorodumi

  • In 15th Sep 2016, the development versions of EM Navigator and Yorodumi will replace the official versions.
  • Current version will continue as 'legacy version' for some time.

Related info.: Changes in new EM Navigator and Yorodumi / EM Navigator / Yorodumi

Read more

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.

Related info.: EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more