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- PDB-8z3o: Cryo-EM structure of the receptor of hGPR68-Gs complex in pH6.0 -

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Basic information

Entry
Database: PDB / ID: 8z3o
TitleCryo-EM structure of the receptor of hGPR68-Gs complex in pH6.0
ComponentsOvarian cancer G-protein coupled receptor 1
KeywordsMEMBRANE PROTEIN / pH6.0 / hGPR68 / MEMBRANE PROTE
Function / homology
Function and homology information


positive regulation of osteoclast development / cellular response to pH / negative regulation of monocyte differentiation / osteoclast development / Class A/1 (Rhodopsin-like receptors) / insulin secretion / monocyte differentiation / positive regulation of insulin secretion involved in cellular response to glucose stimulus / G protein-coupled receptor activity / G alpha (q) signalling events ...positive regulation of osteoclast development / cellular response to pH / negative regulation of monocyte differentiation / osteoclast development / Class A/1 (Rhodopsin-like receptors) / insulin secretion / monocyte differentiation / positive regulation of insulin secretion involved in cellular response to glucose stimulus / G protein-coupled receptor activity / G alpha (q) signalling events / G protein-coupled receptor signaling pathway / inflammatory response / plasma membrane
Similarity search - Function
OGR1 sphingosylphosphorylcholine receptor / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family)
Similarity search - Domain/homology
G-protein coupled receptor 68
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsZhong, Y.N. / Guo, L.L.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)81773704 China
CitationJournal: To Be Published
Title: Cryo-EM structure of the receptor of hGPR68-Gs complex in pH6.0
Authors: Zhong, Y.N. / Guo, L.L.
History
DepositionApr 15, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Apr 23, 2025Provider: repository / Type: Initial release
Revision 1.0Apr 23, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Apr 23, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Apr 23, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Apr 23, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Apr 23, 2025Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Apr 23, 2025Data 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
R: Ovarian cancer G-protein coupled receptor 1


Theoretical massNumber of molelcules
Total (without water)36,5111
Polymers36,5111
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Ovarian cancer G-protein coupled receptor 1 / G-protein coupled receptor 68 / OGR-1 / GPR12A / Sphingosylphosphorylcholine receptor


Mass: 36511.469 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GPR68, OGR1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q15743
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: Cryo-EM structure of the receptor of hGPR68-Gs complex in pH6.0
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 6
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DIFFRACTION / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 1.875 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 134460 / Symmetry type: POINT

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