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- PDB-9y2f: Metabotropic Glutamate Receptor 7 in complex with ecto-domain of ... -

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Basic information

Entry
Database: PDB / ID: 9y2f
TitleMetabotropic Glutamate Receptor 7 in complex with ecto-domain of Extracellular Leucine Rich Repeat and Fibronectin Type III Domain Containing 2
Components
  • Metabotropic glutamate receptor 7
  • Protein phosphatase 1 regulatory subunit 29
KeywordsMEMBRANE PROTEIN / mGluR7 / ELFN2 / GPCR / glutamate / trans-synaptic
Function / homology
Function and homology information


group III metabotropic glutamate receptor activity / negative regulation of glutamate secretion / adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway / serine binding / synaptic membrane adhesion / G protein-coupled glutamate receptor signaling pathway / Class C/3 (Metabotropic glutamate/pheromone receptors) / glutamate receptor activity / presynaptic active zone / glutamate binding ...group III metabotropic glutamate receptor activity / negative regulation of glutamate secretion / adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway / serine binding / synaptic membrane adhesion / G protein-coupled glutamate receptor signaling pathway / Class C/3 (Metabotropic glutamate/pheromone receptors) / glutamate receptor activity / presynaptic active zone / glutamate binding / protein phosphatase inhibitor activity / axon development / asymmetric synapse / regulation of synaptic transmission, glutamatergic / adenylate cyclase inhibitor activity / sensory perception of sound / dendritic shaft / PDZ domain binding / establishment of protein localization / postsynaptic density membrane / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / signaling receptor activity / chemical synaptic transmission / cell cortex / G alpha (i) signalling events / signaling receptor complex / postsynaptic membrane / protein dimerization activity / axon / calcium ion binding / dendrite / : / membrane / plasma membrane
Similarity search - Function
: / ELFN1/ELFN2, fibronectin type-III domain / GPCR, family 3, metabotropic glutamate receptor 7 / : / GPCR, family 3, metabotropic glutamate receptor / : / G-protein coupled receptors family 3 signature 1. / G-protein coupled receptors family 3 signature 3. / G-protein coupled receptors family 3 signature 2. / GPCR, family 3, nine cysteines domain ...: / ELFN1/ELFN2, fibronectin type-III domain / GPCR, family 3, metabotropic glutamate receptor 7 / : / GPCR, family 3, metabotropic glutamate receptor / : / G-protein coupled receptors family 3 signature 1. / G-protein coupled receptors family 3 signature 3. / G-protein coupled receptors family 3 signature 2. / GPCR, family 3, nine cysteines domain / GPCR, family 3, nine cysteines domain superfamily / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, conserved site / GPCR, family 3 / G-protein coupled receptors family 3 profile. / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Receptor, ligand binding region / Receptor family ligand binding region / Leucine-rich repeat domain superfamily / Periplasmic binding protein-like I
Similarity search - Domain/homology
Metabotropic glutamate receptor 7 / Protein phosphatase 1 regulatory subunit 29
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.6 Å
AuthorsLudlam, W.G. / Chang, C.T. / Liauw, B.W. / Cho, H.J. / Sawh-Gopal, A. / Izard, T. / Bao, H. / Dunn, H.A. / Vafabakhsh, R. / Martemyanov, K.A.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Drug Abuse (NIH/NIDA)DA056414 United States
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)F32NS124758 United States
CitationJournal: To Be Published
Title: Structural basis for modulation of group III mGlu receptors by trans-synaptic interactions
Authors: Ludlam, W.G. / Chang, C.T. / Liauw, B.W. / Cho, H.J. / Sawh-Gopal, A. / Izard, T. / Bao, H. / Dunn, H.A. / Vafabakhsh, R. / Martemyanov, K.A.
History
DepositionSep 1, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 5, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 5, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Aug 5, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Aug 5, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 5, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 5, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Aug 5, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
C: Protein phosphatase 1 regulatory subunit 29
A: Metabotropic glutamate receptor 7
D: Protein phosphatase 1 regulatory subunit 29
B: Metabotropic glutamate receptor 7


Theoretical massNumber of molelcules
Total (without water)280,4224
Polymers280,4224
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Protein phosphatase 1 regulatory subunit 29 / Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2 / Leucine- ...Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2 / Leucine-rich repeat and fibronectin type-III domain-containing protein 6 / Leucine-rich repeat-containing protein 62


Mass: 43056.125 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: M1-A22 is cleaved off signal peptide. D23-G248 is leucine rich repeat domain. S249-T379 is not resolved in the structure. L380-Q385 is human rhinovirus C3 protease cut site sequence.
Source: (gene. exp.) Homo sapiens (human) / Gene: ELFN2, KIAA1904, LRRC62, PPP1R29 / Production host: Homo sapiens (human) / References: UniProt: Q5R3F8
#2: Protein Metabotropic glutamate receptor 7 / mGluR7


Mass: 97154.852 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: M1-G34 is cleaved signal peptide. Q35-M37 is not resolved in structure. Y38-S521 is Venus Flytrap domain. V522-R859 is not resolved in structure. L860-Q865 is human rhinovirus C3 protease cut site sequence.
Source: (gene. exp.) Homo sapiens (human) / Gene: GRM7, GPRC1G, MGLUR7 / Production host: Homo sapiens (human) / References: UniProt: Q14831
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Complex of mGluR7 and ecto-domain of ELFN2 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: JEOL CRYO ARM 300
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2PHENIX1.21.2_5419model refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 28023 / Symmetry type: POINT
RefinementHighest resolution: 4.6 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00311156
ELECTRON MICROSCOPYf_angle_d0.53315160
ELECTRON MICROSCOPYf_dihedral_angle_d4.3211530
ELECTRON MICROSCOPYf_chiral_restr0.041686
ELECTRON MICROSCOPYf_plane_restr0.0042000

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