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- EMDB-70965: CryoEM structure of Ggust-coupled TAS2R43 with aristolochic acid I -

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Basic information

Entry
Database: EMDB / ID: EMD-70965
TitleCryoEM structure of Ggust-coupled TAS2R43 with aristolochic acid I
Map data
Sample
  • Complex: GPCR complex 1
    • Protein or peptide: Guanine nucleotide-binding protein G(t) subunit alpha-3
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
    • Protein or peptide: scFv16
    • Protein or peptide: Taste receptor type 2 member 43
  • Ligand: 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid
  • Ligand: water
KeywordsGPCR / SIGNALING PROTEIN
Function / homology
Function and homology information


bitter taste receptor activity / sensory perception of bitter taste / taste receptor activity / sensory perception of umami taste / detection of light stimulus involved in visual perception / sensory perception of sweet taste / detection of chemical stimulus involved in sensory perception of bitter taste / motile cilium / Class C/3 (Metabotropic glutamate/pheromone receptors) / ciliary membrane ...bitter taste receptor activity / sensory perception of bitter taste / taste receptor activity / sensory perception of umami taste / detection of light stimulus involved in visual perception / sensory perception of sweet taste / detection of chemical stimulus involved in sensory perception of bitter taste / motile cilium / Class C/3 (Metabotropic glutamate/pheromone receptors) / ciliary membrane / phototransduction, visible light / axoneme / Adenylate cyclase inhibitory pathway / acrosomal vesicle / response to nicotine / G protein-coupled receptor binding / G protein-coupled receptor activity / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / Olfactory Signaling Pathway / Activation of the phototransduction cascade / G protein-coupled acetylcholine receptor 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 / photoreceptor disc membrane / ADP signalling through P2Y purinoceptor 12 / Sensory perception of sweet, bitter, and umami (glutamate) taste / Glucagon-type ligand receptors / 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 / cellular response to catecholamine stimulus / ADP signalling through P2Y purinoceptor 1 / ADORA2B mediated anti-inflammatory cytokines production / G beta:gamma signalling through PI3Kgamma / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / cellular response to prostaglandin E stimulus / heterotrimeric G-protein complex / G alpha (12/13) signalling events / Inactivation, recovery and regulation of the phototransduction cascade / G-protein beta-subunit binding / extracellular vesicle / sensory perception of taste / Thrombin signalling through proteinase activated receptors (PARs) / signaling receptor complex adaptor activity / retina development in camera-type eye / GTPase binding / fibroblast proliferation / Ca2+ pathway / 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 / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / Ras protein signal transduction / Extra-nuclear estrogen signaling / cell population proliferation / apical plasma membrane / G protein-coupled receptor signaling pathway / lysosomal membrane / GTPase activity / synapse / GTP binding / protein-containing complex binding / signal transduction / protein-containing complex / extracellular exosome / membrane / metal ion binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
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. ...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 / Taste receptor type 2 member 43 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 / Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsKim Y / Gumpper RH / Roth BL
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)U24 DK116195 United States
CitationJournal: Nat Struct Mol Biol / Year: 2026
Title: Structural insights into coffee bitter taste perception by TAS2R43 receptor.
Authors: Yoojoong Kim / Ryan H Gumpper / Yuxuan Zhuang / Ron O Dror / Bryan L Roth /
Abstract: Bitter taste functions as a means of both protection against potentially toxic compounds and savoring bitter tasting foods and beverages. Among the 26 bitter taste receptors, taste receptor type 2 ...Bitter taste functions as a means of both protection against potentially toxic compounds and savoring bitter tasting foods and beverages. Among the 26 bitter taste receptors, taste receptor type 2 member 43 (TAS2R43) has been identified as key for recognizing the bitter taste of coffee. TAS2R43 has also been implicated in many other physiological processes, including the regulation of glucagon-like peptide 1 release from the intestine, bronchodilation, innate immunity and metabolism. Here we report cryo-electron microscopy structures of human TAS2R43 coupled with inhibitory G protein or gustducin (G) stabilized by the potent nephrotoxin and carcinogen aristolochic acid I. Both structures revealed that aristolochic acid I binds in a presumed orthosteric pocket shared with other bitter taste receptor. Further structural, functional and computational studies revealed potential modes for coffee's constituents including caffeine and cafestol, which are bitter tastants from coffee. Lastly, long-timescale molecular dynamics simulations identified potential cryptic allosteric pockets in TAS2R43. These structures could accelerate the search for specific bitter taste ligands that ultimately may be therapeutically useful.
History
DepositionJun 3, 2025-
Header (metadata) releaseApr 22, 2026-
Map releaseApr 22, 2026-
UpdateMay 6, 2026-
Current statusMay 6, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_70965.png

Downloads & links

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Map

FileDownload / File: emd_70965.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
0.88 Å/pix.
x 288 pix.
= 252.288 Å		0.88 Å/pix.
x 288 pix.
= 252.288 Å		0.88 Å/pix.
x 288 pix.
= 252.288 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.876 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.55
Minimum - Maximum-2.4042222 - 5.9672437
Average (Standard dev.)0.023567554 (±0.103370994)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 252.288 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_70965_half_map_1.map
Projections & Slices
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Histogram (log scale)

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Half map: #1

Fileemd_70965_half_map_2.map
Projections & Slices
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Sample components

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Entire : GPCR complex 1

EntireName: GPCR complex 1
Components
  • Complex: GPCR complex 1
    • Protein or peptide: Guanine nucleotide-binding protein G(t) subunit alpha-3
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
    • Protein or peptide: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
    • Protein or peptide: scFv16
    • Protein or peptide: Taste receptor type 2 member 43
  • Ligand: 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid
  • Ligand: water

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Supramolecule #1: GPCR complex 1

SupramoleculeName: GPCR complex 1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Guanine nucleotide-binding protein G(t) subunit alpha-3

MacromoleculeName: Guanine nucleotide-binding protein G(t) subunit alpha-3
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.339848 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGSTVSAEDK AAAERSKMID KNLREDAERD ARTVKLLLLG AGESGKATIV KQQMIIHKNG YSEQECMEFK AVIYSNTLQS ILAIVKAMT TLGIDYVNPR SAEDQRQLYA MANTLEDGGM TPQLAEVIKR LWRDPGIQAC FERASEYQLN DSAAYYLNDL D RITASGYV ...String:
MGSTVSAEDK AAAERSKMID KNLREDAERD ARTVKLLLLG AGESGKATIV KQQMIIHKNG YSEQECMEFK AVIYSNTLQS ILAIVKAMT TLGIDYVNPR SAEDQRQLYA MANTLEDGGM TPQLAEVIKR LWRDPGIQAC FERASEYQLN DSAAYYLNDL D RITASGYV PNEQDVLHSR VKTTGIIETQ FSFKDLHFRM FDVGAQRSER KKWIHCFEGV TCIIFCAALS AYDMVLVEDE EV NRMHASL KLFDSICNHK YFSDTSIVLF LNKKDIFQEK VTKVHLSICF PEYTGPNTFE DAGNYIKNQF LDLNLKKEDK EIY SHMTCS TDTQNVKFVF DAVTDIIIKE NLKDCGLF

UniProtKB: Guanine nucleotide-binding protein G(t) subunit alpha-3

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Macromolecule #2: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

MacromoleculeName: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 42.936668 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MHHHHHHLEV LFQGPGSSGS ELDQLRQEAE QLKNQIRDAR KACADATLSQ ITNNIDPVGR IQMRTRRTLR GHLAKIYAMH WGTDSRLLV SASQDGKLII WDSYTTNKVH AIPLRSSWVM TCAYAPSGNY VACGGLDNIC SIYNLKTREG NVRVSRELAG H TGYLSCCR ...String:
MHHHHHHLEV LFQGPGSSGS ELDQLRQEAE QLKNQIRDAR KACADATLSQ ITNNIDPVGR IQMRTRRTLR GHLAKIYAMH WGTDSRLLV SASQDGKLII WDSYTTNKVH AIPLRSSWVM TCAYAPSGNY VACGGLDNIC SIYNLKTREG NVRVSRELAG H TGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TF TGHESDI NAICFFPNGN AFATGSDDAT CRLFDLRADQ ELMTYSHDNI ICGITSVSFS KSGRLLLAGY DDFNCNVWDA LKA DRAGVL AGHDNRVSCL GVTDDGMAVA TGSWDSFLKI WNGGSGGGGS GGSSSGGGGS GGGGSGGSSS GGVSGWRLFK KISG GS

UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

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Macromolecule #3: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

MacromoleculeName: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.861143 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP FREKKFFCAI L

UniProtKB: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

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Macromolecule #4: scFv16

MacromoleculeName: scFv16 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.668922 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: DVQLVESGGG LVQPGGSRKL SCSASGFAFS SFGMHWVRQA PEKGLEWVAY ISSGSGTIYY ADTVKGRFTI SRDDPKNTLF LQMTSLRSE DTAMYYCVRS IYYYGSSPFD FWGQGTTLTV SSGGGGSGGG GSGGGGSDIV MTQATSSVPV TPGESVSISC R SSKSLLHS ...String:
DVQLVESGGG LVQPGGSRKL SCSASGFAFS SFGMHWVRQA PEKGLEWVAY ISSGSGTIYY ADTVKGRFTI SRDDPKNTLF LQMTSLRSE DTAMYYCVRS IYYYGSSPFD FWGQGTTLTV SSGGGGSGGG GSGGGGSDIV MTQATSSVPV TPGESVSISC R SSKSLLHS NGNTYLYWFL QRPGQSPQLL IYRMSNLASG VPDRFSGSGS GTAFTLTISR LEAEDVGVYY CMQHLEYPLT FG AGTKLEL KAAALEVLFQ GPHHHHHHHH

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Macromolecule #5: Taste receptor type 2 member 43

MacromoleculeName: Taste receptor type 2 member 43 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.130312 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: DYKDDDDAKL QTMHHHHHHH HHHENLYFQG GTTMADLEDN WETLNDNLKV IEKADNAAQV KDALTKMRAA ALDAQKATPP KLEDKSPDS PEMKDFRHGF DILVGQIDDA LKLANEGKVK EAQAAAEQLK TTRNAYIQKY LGSTLEVLFQ GPMITFLPII F SSLVVVTF ...String:
DYKDDDDAKL QTMHHHHHHH HHHENLYFQG GTTMADLEDN WETLNDNLKV IEKADNAAQV KDALTKMRAA ALDAQKATPP KLEDKSPDS PEMKDFRHGF DILVGQIDDA LKLANEGKVK EAQAAAEQLK TTRNAYIQKY LGSTLEVLFQ GPMITFLPII F SSLVVVTF VIGNFANGFI ALVNSIEWFK RQKISFADQI LTALAVSRVG LLWVLLLNWY STVLNPAFNS VEVRTTAYNI WA VINHFSN WLATTLSIFY LLKIANFSNF IFLHLKRRVK SVILVMLLGP LLFLACHLFV INMNEIVRTK EFEGNMTWKI KLK SAMYFS NMTVTMVANL VPFTLTLLSF MLLICSLCKH LKKMQLHGKG SQDPSTKVHI KALQTVISFL LLCAIYFLSI MISV WSFGS LENKPVFMFC KAIRFSYPSI HPFILIWGNK KLKQTFLSVF WQMRYWVKGE KTSSPGSAGS AGSGGSGGGS GGGGS GGSS SGGVFTLEDF VGDWEQTAAY NLDQVLEQGG VSSLLQNLAV SVTPIQRIVR SGENALKIDI HVIIPYEGLS ADQMAQ IEE VFKVVYPVDD HHFKVILPYG TLVIDGVTPN MLNYFGRPYE GIAVFDGKKI TVTGTLWNGN KIIDERLITP DGSMLFR VT INS

UniProtKB: Taste receptor type 2 member 43

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Macromolecule #6: 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid

MacromoleculeName: 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid
type: ligand / ID: 6 / Number of copies: 1 / Formula: GOQ
Molecular weightTheoretical: 341.272 Da
Chemical component information

ChemComp-GOQ:
8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid

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Macromolecule #7: water

MacromoleculeName: water / type: ligand / ID: 7 / Number of copies: 5 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration7 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 95 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 20.0 µm / Nominal defocus min: 5.0 µm
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

8vy9

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 471455
Initial angle assignmentType: OTHER / Details: cryoSPARC ab-initio
Final angle assignmentType: ANGULAR RECONSTITUTION

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