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- EMDB-35377: Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (loca... -
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Open data
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Basic information
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Title | Cryo-EM structure of GPR156 of GPR156-miniGo-scFv16 complex (local refine) | |||||||||
![]() | GPCR | |||||||||
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![]() | Membrane protein / G-protein coupled receptor / Signal transduction / Phospholipid / SIGNALING PROTEIN | |||||||||
Function / homology | ![]() G protein-coupled GABA receptor activity / G protein-coupled receptor heterodimeric complex / gamma-aminobutyric acid signaling pathway / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.03 Å | |||||||||
![]() | Shin J / Park J / Cho Y | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Constitutive activation mechanism of a class C GPCR. Authors: Jinwoo Shin / Junhyeon Park / Jieun Jeong / Jordy Homing Lam / Xingyu Qiu / Di Wu / Kuglae Kim / Joo-Youn Lee / Carol V Robinson / Jaekyung Hyun / Vsevolod Katritch / Kwang Pyo Kim / Yunje Cho / ![]() ![]() ![]() Abstract: Class C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a ...Class C G-protein-coupled receptors (GPCRs) are activated through binding of agonists to the large extracellular domain (ECD) followed by rearrangement of the transmembrane domains (TMDs). GPR156, a class C orphan GPCR, is unique because it lacks an ECD and exhibits constitutive activity. Impaired GPR156-G signaling contributes to loss of hearing. Here we present the cryo-electron microscopy structures of human GPR156 in the G-free and G-coupled states. We found that an endogenous phospholipid molecule is located within each TMD of the GPR156 dimer. Asymmetric binding of Gα to the phospholipid-bound GPR156 dimer restructures the first and second intracellular loops and the carboxy-terminal part of the elongated transmembrane 7 (TM7) without altering dimer conformation. Our findings reveal that GPR156 is a transducer for phospholipid signaling. Constant binding of abundant phospholipid molecules and the G-protein-induced reshaping of the cytoplasmic face provide a basis for the constitutive activation of GPR156. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 234.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.2 KB 14.2 KB | Display Display | ![]() |
Images | ![]() | 120.8 KB | ||
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 243.7 MB 243.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8iebMC ![]() 8iecC ![]() 8iedC ![]() 8ieiC ![]() 8iepC ![]() 8ieqC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | GPCR | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.81 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_35377_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_35377_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : GPR156
Entire | Name: GPR156 |
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Components |
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-Supramolecule #1: GPR156
Supramolecule | Name: GPR156 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 131.2 kDa/nm |
-Macromolecule #1: Probable G-protein coupled receptor 156
Macromolecule | Name: Probable G-protein coupled receptor 156 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 65.628484 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MEPEINCSEL CDSFPGQELD RRPLHDLCKT TITSSHHSSK TISSLSPVLL GIVWTFLSCG LLLILFFLAF TIHCRKNRIV KMSSPNLNI VTLLGSCLTY SSAYLFGIQD VLVGSSMETL IQTRLSMLCI GTSLVFGPIL GKSWRLYKVF TQRVPDKRVI I KDLQLLGL ...String: MEPEINCSEL CDSFPGQELD RRPLHDLCKT TITSSHHSSK TISSLSPVLL GIVWTFLSCG LLLILFFLAF TIHCRKNRIV KMSSPNLNI VTLLGSCLTY SSAYLFGIQD VLVGSSMETL IQTRLSMLCI GTSLVFGPIL GKSWRLYKVF TQRVPDKRVI I KDLQLLGL VAALLMADVI LLMTWVLTDP IQCLQILSVS MTVTGKDVSC TSTSTHFCAS RYSDVWIALI WGCKGLLLLY GA YLAGLTG HVSSPPVNQS LTIMVGVNLL VLAAGLLFVV TRYLHSWPNL VFGLTSGGIF VCTTTINCFI FIPQLKQWKA FEE ENQTIR RMAKYFSTPN KSFHTQYGEE ENCHPRGEKS SMERLLTEKN AVIESLQEQV NNAKEKIVRL MSAECTYDLP EGAA PPASS PNKDVQAVAS VHTLAAAQGP SGHLSDFQND PGMAARDSQC TSGPSSYAQS LEGPGKDSSF SPGKEEKISD SKDFS DHLD SGCSQKPWTE QSLGPERGDQ VPMNPSQSLL PERGGSDPQR QRHLENSEEP PERRSRVSSV IREKLQEVLQ DLGSGS GSG RGRGGSENLY FQGGSGSGGD YKDDDDKDYK DDDDK UniProtKB: Probable G-protein coupled receptor 156 |
-Macromolecule #2: [(2R)-3-[(E)-hexadec-9-enoyl]oxy-2-octadecanoyloxy-propyl] 2-(tri...
Macromolecule | Name: [(2R)-3-[(E)-hexadec-9-enoyl]oxy-2-octadecanoyloxy-propyl] 2-(trimethylazaniumyl)ethyl phosphate type: ligand / ID: 2 / Number of copies: 2 / Formula: A1LYA |
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Molecular weight | Theoretical: 760.076 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 64.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: OTHER |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL / In silico model: AlphaFold2 |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 205728 |
Initial angle assignment | Type: OTHER |
Final angle assignment | Type: OTHER |