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- PDB-7ewr: Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in ... -
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Basic information
Entry | Database: PDB / ID: 7ewr | ||||||||||||
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Title | Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio | ||||||||||||
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![]() | SIGNALING PROTEIN / GPCR | ||||||||||||
Function / homology | ![]() G protein-coupled glycine receptor activity / GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / negative regulation of G protein-coupled receptor signaling pathway / positive regulation of potassium ion transmembrane transport / regulation of G protein-coupled receptor signaling pathway / positive regulation of neurotransmitter secretion ...G protein-coupled glycine receptor activity / GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / negative regulation of G protein-coupled receptor signaling pathway / positive regulation of potassium ion transmembrane transport / regulation of G protein-coupled receptor signaling pathway / positive regulation of neurotransmitter secretion / G protein-coupled dopamine receptor signaling pathway / regulation of synapse organization / G-protein alpha-subunit binding / enzyme activator activity / response to amphetamine / GTPase activator activity / positive regulation of GTPase activity / cell projection / protein localization to plasma membrane / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G-protein activation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / brain development / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / cognition / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / transmembrane signaling receptor activity / G-protein beta-subunit binding / Inactivation, recovery and regulation of the phototransduction cascade / heterotrimeric G-protein complex / G alpha (12/13) signalling events / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / presynapse / presynaptic membrane / Ca2+ pathway / nuclear envelope / G alpha (i) signalling events / protein-folding chaperone binding / G alpha (s) signalling events / G alpha (q) signalling events / postsynaptic membrane / response to ethanol / Extra-nuclear estrogen signaling / intracellular signal transduction / neuron projection / G protein-coupled receptor signaling pathway / GTPase activity / signal transduction / protein-containing complex / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.7 Å | ||||||||||||
![]() | Kim, Y. / Jeong, E. / Jeong, J. / Cho, Y. | ||||||||||||
Funding support | 3items
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![]() | ![]() Title: Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. Authors: Eunyoung Jeong / Yoojoong Kim / Jihong Jeong / Yunje Cho / ![]() Abstract: GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding ...GPR158, a class C orphan GPCR, functions in cognition, stress-induced mood control, and synaptic development. Among class C GPCRs, GPR158 is unique as it lacks a Venus flytrap-fold ligand-binding domain and terminates Gαi/o protein signaling through the RGS7-Gβ5 heterodimer. Here, we report the cryo-EM structures of GPR158 alone and in complex with one or two RGS7-Gβ5 heterodimers. GPR158 dimerizes through Per-Arnt-Sim-fold extracellular and transmembrane (TM) domains connected by an epidermal growth factor-like linker. The TM domain (TMD) reflects both inactive and active states of other class C GPCRs: a compact intracellular TMD, conformations of the two intracellular loops (ICLs) and the TMD interface formed by TM4/5. The ICL2, ICL3, TM3, and first helix of the cytoplasmic coiled-coil provide a platform for the DHEX domain of one RGS7 and the second helix recruits another RGS7. The unique features of the RGS7-binding site underlie the selectivity of GPR158 for RGS7. | ||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 771.2 KB | Display | ![]() |
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PDB format | ![]() | 614.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 853.8 KB | Display | ![]() |
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Full document | ![]() | 983.2 KB | Display | |
Data in XML | ![]() | 86.5 KB | Display | |
Data in CIF | ![]() | 128.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 31363MC ![]() 7ewlC ![]() 7ewpC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 61570.086 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 43619.297 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Protein | Mass: 127547.109 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:2:2 ratio Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: C-flat-1.2/1.3 |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Microscopy | Model: FEI TALOS ARCTICA |
Electron gun | Electron source: ![]() |
Electron lens | Mode: DIFFRACTION |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.14-3260_1069: / Classification: refinement |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
3D reconstruction | Resolution: 4.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 236504 / Symmetry type: POINT |