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- PDB-9uta: The transmembrane domains of human sweet taste receptor TAS1R2 an... -

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Basic information

Entry
Database: PDB / ID: 9uta
TitleThe transmembrane domains of human sweet taste receptor TAS1R2 and TAS1R3 in the apo state
Components
  • Taste receptor type 1 member 2,Engineered red fluorescent protein mScarlet3
  • Taste receptor type 1 member 3,mNeonGreen
KeywordsSIGNALING PROTEIN / GPCR / Taste / Tas1R2 / Tas1R3
Function / homology
Function and homology information


sweet taste receptor complex / detection of chemical stimulus involved in sensory perception of sweet taste / sweet taste receptor activity / taste receptor activity / sensory perception of umami taste / sensory perception of sweet taste / Class C/3 (Metabotropic glutamate/pheromone receptors) / positive regulation of cytokinesis / bioluminescence / G protein-coupled receptor activity ...sweet taste receptor complex / detection of chemical stimulus involved in sensory perception of sweet taste / sweet taste receptor activity / taste receptor activity / sensory perception of umami taste / sensory perception of sweet taste / Class C/3 (Metabotropic glutamate/pheromone receptors) / positive regulation of cytokinesis / bioluminescence / G protein-coupled receptor activity / Sensory perception of sweet, bitter, and umami (glutamate) taste / G alpha (i) signalling events / receptor complex / G protein-coupled receptor signaling pathway / Golgi apparatus / membrane / plasma membrane
Similarity search - Function
GPCR, family 3, extracellular calcium-sensing receptor-related / G-protein coupled receptors family 3 signature 2. / GPCR, family 3, nine cysteines domain / GPCR, family 3, nine cysteines domain superfamily / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, conserved site / GPCR, family 3 / G-protein coupled receptors family 3 profile. / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR ...GPCR, family 3, extracellular calcium-sensing receptor-related / G-protein coupled receptors family 3 signature 2. / GPCR, family 3, nine cysteines domain / GPCR, family 3, nine cysteines domain superfamily / Nine Cysteines Domain of family 3 GPCR / GPCR, family 3, conserved site / GPCR, family 3 / G-protein coupled receptors family 3 profile. / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I
Similarity search - Domain/homology
mNeonGreen / Taste receptor type 1 member 3 / Taste receptor type 1 member 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Discosoma sp. (sea anemone)
Branchiostoma lanceolatum (amphioxus)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.77 Å
AuthorsShi, Z.J. / Xu, W.X. / Yue, X.L. / Wu, L.J. / Hua, T. / Liu, Z.J.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nature / Year: 2025
Title: Structural and functional characterization of human sweet taste receptor.
Authors: Zongjun Shi / Weixiu Xu / Lijie Wu / Xiaolei Yue / Shenhui Liu / Wei Ding / Jinyi Zhang / Bing Meng / Lianghao Zhao / Xiaoyan Liu / Junlin Liu / Zhi-Jie Liu / Tian Hua /
Abstract: Sweet taste perception influences dietary choices and metabolic health. The human sweet taste receptor, a class C G protein-coupled receptor (GPCR) heterodimer composed of TAS1R2-TAS1R3, senses a ...Sweet taste perception influences dietary choices and metabolic health. The human sweet taste receptor, a class C G protein-coupled receptor (GPCR) heterodimer composed of TAS1R2-TAS1R3, senses a wide range of sweet compounds - including natural sugars, artificial sweeteners and sweet proteins - impacting metabolic regulation beyond taste. However, the lack of three-dimensional structures hinders our understanding of its precise working mechanism. Here, we present cryo-EM structures of the full-length human sweet taste receptor in apo- and sucralose-bound states. These structures reveal a distinct asymmetric heterodimer architecture, with sucralose binding exclusively to the Venus flytrap domain of TAS1R2. Combining mutagenesis and molecular dynamics simulations, this work delineates the sweeteners recognition modes in TAS1R2. Structural comparisons further uncover the conformational changes upon ligand binding and unique activation mechanism. These findings illuminate the signal transduction mechanisms of chemosensory receptors in class C GPCRs and provide molecular basis for new-generation sweetener design.
History
DepositionMay 3, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 16, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Taste receptor type 1 member 2,Engineered red fluorescent protein mScarlet3
B: Taste receptor type 1 member 3,mNeonGreen


Theoretical massNumber of molelcules
Total (without water)247,0982
Polymers247,0982
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 Taste receptor type 1 member 2,Engineered red fluorescent protein mScarlet3 / G-protein coupled receptor 71 / Sweet taste receptor T1R2


Mass: 122191.227 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Engineered red fluorescent protein mScarlet3: PMID: 27869816 and PDB ID: 7ZCT
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Discosoma sp. (Sea anemone) (sea anemone)
Gene: TAS1R2, GPR71, T1R2, TR2 / Production host: Homo sapiens (human) / References: UniProt: Q8TE23
#2: Protein Taste receptor type 1 member 3,mNeonGreen / Sweet taste receptor T1R3


Mass: 124906.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Branchiostoma lanceolatum (amphioxus)
Gene: TAS1R3, T1R3, TR3, blFP-Y3 / Production host: Homo sapiens (human) / References: UniProt: Q7RTX0, UniProt: A0A1S4NYF2
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: heterodimer / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company
MicroscopyModel: FEI TALOS ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.20.1_4487 / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 70080 / Symmetry type: POINT
RefinementHighest resolution: 3.77 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0054834
ELECTRON MICROSCOPYf_angle_d0.7096607
ELECTRON MICROSCOPYf_dihedral_angle_d4.921650
ELECTRON MICROSCOPYf_chiral_restr0.039778
ELECTRON MICROSCOPYf_plane_restr0.008815

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