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Yorodumi- EMDB-36421: The cryo-EM structure of insect gustatory receptor Gr64a from Dro... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-36421 | |||||||||
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Title | The cryo-EM structure of insect gustatory receptor Gr64a from Drosophila melanogaster in complex with sucrose | |||||||||
Map data | ||||||||||
Sample |
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Keywords | gustatory receptor / Gr64a / sucrose / ligand-gated ion channel / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information proboscis extension reflex / detection of chemical stimulus involved in sensory perception of taste / sweet taste receptor activity / taste receptor activity / sensory perception of sweet taste / ligand-gated monoatomic ion channel activity / monoatomic ion transmembrane transport / sensory perception of taste / signal transduction / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | Drosophila melanogaster (fruit fly) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.5 Å | |||||||||
Authors | Ma D / Guo J | |||||||||
Funding support | China, 1 items
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Citation | Journal: Science / Year: 2024 Title: Structural basis for sugar perception by gustatory receptors. Authors: Demin Ma / Meiqin Hu / Xiaotong Yang / Qiang Liu / Fan Ye / Weijie Cai / Yong Wang / Ximing Xu / Shenghai Chang / Ruiying Wang / Wei Yang / Sheng Ye / Nannan Su / Minrui Fan / Haoxing Xu / Jiangtao Guo / Abstract: Insects rely on a family of seven transmembrane proteins called gustatory receptors (GRs) to encode different taste modalities, such as sweet and bitter. We report structures of sweet taste ...Insects rely on a family of seven transmembrane proteins called gustatory receptors (GRs) to encode different taste modalities, such as sweet and bitter. We report structures of sweet taste receptors GR43a and GR64a in the apo and sugar-bound states. Both GRs form tetrameric sugar-gated cation channels composed of one central pore domain (PD) and four peripheral ligand-binding domains (LBDs). Whereas GR43a is specifically activated by the monosaccharide fructose that binds to a narrow pocket in LBDs, disaccharides sucrose and maltose selectively activate GR64a by binding to a larger and flatter pocket in LBDs. Sugar binding to LBDs induces local conformational changes, which are subsequently transferred to the PD to cause channel opening. Our studies reveal a structural basis for sugar recognition and activation of GRs. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_36421.map.gz | 45.2 MB | EMDB map data format | |
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Header (meta data) | emd-36421-v30.xml emd-36421.xml | 14.3 KB 14.3 KB | Display Display | EMDB header |
Images | emd_36421.png | 40.9 KB | ||
Filedesc metadata | emd-36421.cif.gz | 5.7 KB | ||
Others | emd_36421_half_map_1.map.gz emd_36421_half_map_2.map.gz | 42.8 MB 42.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-36421 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36421 | HTTPS FTP |
-Validation report
Summary document | emd_36421_validation.pdf.gz | 766 KB | Display | EMDB validaton report |
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Full document | emd_36421_full_validation.pdf.gz | 765.5 KB | Display | |
Data in XML | emd_36421_validation.xml.gz | 11.8 KB | Display | |
Data in CIF | emd_36421_validation.cif.gz | 13.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36421 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36421 | HTTPS FTP |
-Related structure data
Related structure data | 8jmhMC 8jm9C 8jmaC 8jmeC 8jmiC 8x82C 8x83C 8x84C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_36421.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 0.93 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_36421_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_36421_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : gustatory receptor Gr64a
Entire | Name: gustatory receptor Gr64a |
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Components |
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-Supramolecule #1: gustatory receptor Gr64a
Supramolecule | Name: gustatory receptor Gr64a / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
-Macromolecule #1: Gustatory receptor for sugar taste 64a
Macromolecule | Name: Gustatory receptor for sugar taste 64a / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Molecular weight | Theoretical: 54.66825 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MWSHPQFEKG GSSGGVDMKG PNLNFRKTPS KDNGVKQVES LARPETPPPK FVEDSNLEFN VLASEKLPNY TNLDLFHRAV FPFMFLAQC VAIMPLVGIR ESNPRRVRFA YKSIPMFVTL IFMIATSILF LSMFTHLLKI GITAKNFVGL VFFGCVLSAY V VFIRLAKK ...String: MWSHPQFEKG GSSGGVDMKG PNLNFRKTPS KDNGVKQVES LARPETPPPK FVEDSNLEFN VLASEKLPNY TNLDLFHRAV FPFMFLAQC VAIMPLVGIR ESNPRRVRFA YKSIPMFVTL IFMIATSILF LSMFTHLLKI GITAKNFVGL VFFGCVLSAY V VFIRLAKK WPAVVRIWTR TEIPFTKPPY EIPKRNLSRR VQLAALAIIG LSLGEHALYQ VSAILSYTRR IQMCANITTV PS FNNYMQT NYDYVFQLLP YSPIIAVLIL LINGACTFVW NYMDLFIMMI SKGLSYRFEQ ITTRIRKLEH EEVCESVFIQ IRE HYVKMC ELLEFVDSAM SSLILLSCVN NLYFVCYQLL NVFNKLRWPI NYIYFWYSLL YLIGRTAFVF LTAADINEES KRGL GVLRR VSSRSWCVEV ERLIFQMTTQ TVALSGKKFY FLTRRLLFGM AGTIVTYELV LLQFDEPNRR KGLQPLCA UniProtKB: Gustatory receptor for sugar taste 64a |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-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: 52.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 632430 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |