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- PDB-25su: cryo-EM structure of human TAS2R4 -

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Basic information

Entry
Database: PDB / ID: 25su
Titlecryo-EM structure of human TAS2R4
Components
  • Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
  • Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
  • Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(t) subunit alpha-3
  • Single-chain variable fragment 16
  • Taste receptor type 2 member 4
KeywordsMEMBRANE PROTEIN / bitter taste receptors / cryo-EM
Function / homology
Function and homology information


regulation of phospholipid metabolic process / regulation of hormone metabolic process / regulation of triglyceride metabolic process / bitter taste receptor activity / taste receptor activity / detection of light stimulus involved in visual perception / sensory perception of sweet taste / detection of chemical stimulus involved in sensory perception of bitter taste / regulation of fat cell differentiation / cell volume homeostasis ...regulation of phospholipid metabolic process / regulation of hormone metabolic process / regulation of triglyceride metabolic process / bitter taste receptor activity / taste receptor activity / detection of light stimulus involved in visual perception / sensory perception of sweet taste / detection of chemical stimulus involved in sensory perception of bitter taste / regulation of fat cell differentiation / cell volume homeostasis / Class C/3 (Metabotropic glutamate/pheromone receptors) / regulation of cholesterol metabolic process / ciliary membrane / spectrin binding / regulation of glucose metabolic process / phototransduction, visible light / axoneme / regulation of eating behavior / adenylate cyclase inhibitor activity / positive regulation of protein localization to cell cortex / T cell migration / positive regulation of relaxation of smooth muscle / Adenylate cyclase inhibitory pathway / D2 dopamine receptor binding / adenylate cyclase-inhibiting serotonin receptor signaling pathway / G protein-coupled serotonin receptor binding / acrosomal vesicle / cellular response to forskolin / mast cell degranulation / regulation of mitotic spindle organization / chemokine-mediated signaling pathway / response to nicotine / Regulation of insulin secretion / neuropeptide signaling pathway / response to prostaglandin E / positive regulation of cholesterol biosynthetic process / G protein-coupled receptor binding / regulation of blood pressure / response to peptide hormone / G protein-coupled receptor activity / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / Olfactory Signaling Pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / Prostacyclin signalling through prostacyclin receptor / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / G beta:gamma signalling through BTK / GDP binding / ADP signalling through P2Y purinoceptor 12 / Glucagon-type ligand receptors / Sensory perception of sweet, bitter, and umami (glutamate) taste / 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 / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / ADORA2B mediated anti-inflammatory cytokines production / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / heterotrimeric G-protein complex / G alpha (12/13) signalling events / G-protein beta-subunit binding / sensory perception of taste / Thrombin signalling through proteinase activated receptors (PARs) / signaling receptor complex adaptor activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / regulation of gene expression / cell body / GTPase binding / G protein activity / midbody / Ca2+ pathway / cell cortex / 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 / G alpha (q) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Extra-nuclear estrogen signaling / apical plasma membrane / ciliary basal body / G protein-coupled receptor signaling pathway / cell division / lysosomal membrane / GTPase activity / centrosome / dendrite / synapse / GTP binding / magnesium ion binding
Similarity search - Function
Taste receptor type 2 member 4 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13 / Taste receptor type 2 / Taste receptor protein (TAS2R) / G-protein alpha subunit, group I / G protein alpha subunit, helical insertion / G protein alpha subunit / Guanine nucleotide binding protein (G-protein), alpha subunit / G-protein alpha subunit / G-alpha domain profile. ...Taste receptor type 2 member 4 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13 / Taste receptor type 2 / Taste receptor protein (TAS2R) / G-protein alpha subunit, group I / G protein alpha subunit, helical insertion / G protein alpha subunit / Guanine nucleotide binding protein (G-protein), alpha subunit / G-protein alpha subunit / G-alpha domain profile. / G-protein, gamma subunit / G-protein gamma subunit domain profile. / G-protein gamma-like domain / G-protein gamma-like domain superfamily / GGL domain / G protein gamma subunit-like motifs / GGL domain / G protein beta WD-40 repeat protein / Guanine nucleotide-binding protein, beta subunit / G-protein, beta subunit / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Guanine nucleotide-binding protein G(t) subunit alpha-3 / Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 / Guanine nucleotide-binding protein G(i) subunit alpha-1 / Taste receptor type 2 member 4 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsTan, M. / Wu, J.
Funding support China, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, China) China
CitationJournal: To Be Published
Title: Receptor hyper-flexibility of human bitter receptor TAS2R4 revealed by cryo-EM structures in apo and tripeptide-bound states
Authors: Tan, M. / Wu, J.
History
DepositionApr 16, 2026Deposition site: PDBJ / Processing site: PDBC
SupersessionJul 15, 2026ID: 9M8L
Revision 1.0Jul 15, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
R: Taste receptor type 2 member 4
N: Single-chain variable fragment 16
G: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
B: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
A: Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(t) subunit alpha-3


Theoretical massNumber of molelcules
Total (without water)147,6165
Polymers147,6165
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 2 member 4 / T2R4


Mass: 40987.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TAS2R4 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9NYW5
#2: Antibody Single-chain variable fragment 16


Mass: 33013.008 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Spodoptera frugiperda (fall armyworm)
#3: Protein Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13


Mass: 7959.299 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNG13 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9P2W3
#4: Protein Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 / Transducin beta chain 3


Mass: 38587.559 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNB3 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P16520
#5: Protein Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(t) subunit alpha-3 / Adenylate cyclase-inhibiting G alpha protein / Gustducin alpha-3 chain


Mass: 27068.969 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNAI1, GNAT3 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P63096, UniProt: A8MTJ3, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
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: apo-TAS2R4-miniGgust / Type: COMPLEX / Entity ID: #5, #4, #3, #2, #1 / Source: RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
21Homo sapiens (human)9606
31Mus musculus (house mouse)10090
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.5
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: 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: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION5particle selection
2PHENIX1.21.2_5419model refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 8249282 / Symmetry type: POINT
RefinementHighest resolution: 3.3 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0029173
ELECTRON MICROSCOPYf_angle_d0.47812398
ELECTRON MICROSCOPYf_dihedral_angle_d4.3021231
ELECTRON MICROSCOPYf_chiral_restr0.0391416
ELECTRON MICROSCOPYf_plane_restr0.0031552

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