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Open data
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Basic information
| Entry | Database: PDB / ID: 9v0u | ||||||
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| Title | GPR133-Gain-miniG13 complex | ||||||
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Keywords | MEMBRANE PROTEIN / GPCR / G12/G13 / Complex / Stachel | ||||||
| Function / homology | Function and homology informationD5 dopamine receptor binding / regulation of skeletal muscle contraction / regulation of fibroblast migration / Rho-activating G protein-coupled receptor signaling pathway / regulation of small GTPase mediated signal transduction / NRAGE signals death through JNK / branching involved in blood vessel morphogenesis / CDC42 GTPase cycle / regulation of postsynapse assembly / Rho protein signal transduction ...D5 dopamine receptor binding / regulation of skeletal muscle contraction / regulation of fibroblast migration / Rho-activating G protein-coupled receptor signaling pathway / regulation of small GTPase mediated signal transduction / NRAGE signals death through JNK / branching involved in blood vessel morphogenesis / CDC42 GTPase cycle / regulation of postsynapse assembly / Rho protein signal transduction / RAC1 GTPase cycle / guanyl-nucleotide exchange factor activity / brush border membrane / G protein-coupled receptor activity / platelet activation / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / regulation of blood pressure / G-protein beta/gamma-subunit complex binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / adenylate cyclase-activating G protein-coupled receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G protein-coupled acetylcholine receptor signaling pathway / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / ADP signalling through P2Y purinoceptor 12 / photoreceptor disc membrane / Sensory perception of sweet, bitter, and umami (glutamate) taste / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (z) signalling events / cellular response to catecholamine stimulus / ADP signalling through P2Y purinoceptor 1 / ADORA2B mediated anti-inflammatory cytokines production / G beta:gamma signalling through PI3Kgamma / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / melanosome / GPER1 signaling / Inactivation, recovery and regulation of the phototransduction cascade / cellular response to prostaglandin E stimulus / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / sensory perception of taste / extracellular vesicle / regulation of cell shape / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / retina development in camera-type eye / G protein activity / GTPase binding / Ca2+ pathway / fibroblast proliferation / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / in utero embryonic development / Ras protein signal transduction / cell differentiation / cell surface receptor signaling pathway / Extra-nuclear estrogen signaling / cell population proliferation / postsynapse / nuclear speck / G protein-coupled receptor signaling pathway / lysosomal membrane / focal adhesion / GTPase activity / synapse / GTP binding / protein-containing complex binding / signal transduction / extracellular exosome / nucleoplasm / metal ion binding / nucleus / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.51 Å | ||||||
Authors | Xi, Y. / Pu, X. / Ping, Y. | ||||||
| Funding support | China, 1items
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Citation | Journal: Biochem Biophys Res Commun / Year: 2025Title: Cryo-EM structural elucidation and molecular mechanism of the GPR133-G13 signaling complex. Authors: Xuanyu Pu / Yue-Tong Xi / Meng-Xin Wang / Daolai Zhang / Yu-Qi Ping / Peng Xiao / Jin-Peng Sun / ![]() Abstract: GPR133 is an adhesion-class G protein-coupled receptor (GPCR) that has recently been de-orphanized. Its functions are complex and multifaceted. While GPR133 is primarily recognized for coupling with ...GPR133 is an adhesion-class G protein-coupled receptor (GPCR) that has recently been de-orphanized. Its functions are complex and multifaceted. While GPR133 is primarily recognized for coupling with the Gs subunit to mediate elevated intracellular cAMP levels, its potential engagement with alternative signaling pathways remains poorly characterized. In our experiments, we demonstrated that GPR133 exhibits constitutive self-activation via its Stachel sequence as an adhesion GPCR, enabling activation of downstream G13 signaling. We reconstituted the GPR133-GAIN-miniGα13 complex in vitro and resolved its cryo-electron microscopy structure at a resolution of 3.51 Å. Detailed structural comparisons between the GPR133-GAIN-miniGα13 complex and the previously resolved GPR133-CTF-Gs structure highlighted both conserved and different features. These findings provide critical insights into the signal transduction mechanisms of GPR133 and lay a foundation for targeted therapeutic strategies. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9v0u.cif.gz | 166.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9v0u.ent.gz | 118.1 KB | Display | PDB format |
| PDBx/mmJSON format | 9v0u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9v0u_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 9v0u_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 9v0u_validation.xml.gz | 34.6 KB | Display | |
| Data in CIF | 9v0u_validation.cif.gz | 51.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/9v0u ftp://data.pdbj.org/pub/pdb/validation_reports/v0/9v0u | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 64672MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 65688.828 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ADGRD1, GPR133, PGR25 / Production host: ![]() |
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| #2: Protein | Mass: 26705.596 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNA13 / Production host: ![]() |
| #3: Protein | Mass: 7861.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNG2 / Production host: ![]() |
| #4: Protein | Mass: 37784.301 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNB1 / Production host: ![]() |
| Has protein modification | Y |
-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: GPR133-Gain-miniG13-Gbeta1-Ggamma2 complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
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| 3D reconstruction | Resolution: 3.51 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 45759 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 74.64 Å2 | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
China, 1items
Citation
PDBj
























FIELD EMISSION GUN