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- EMDB-38584: Structure of human class T GPCR TAS2R14-Gustducin complex with Ar... -

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Entry
Database: EMDB / ID: EMD-38584
TitleStructure of human class T GPCR TAS2R14-Gustducin complex with Aristolochic acid A.
Map data
Sample
  • Complex: Structure of human class T GPCR TAS2R14-Gustducin complex with Aristolochic acid A.
    • 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: Exo-alpha-sialidase,Taste receptor type 2 member 14,LgBiT
    • Protein or peptide: scFv16
  • Ligand: 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid
  • Ligand: CHOLESTEROL
KeywordsGPCR / Gustducin / Tas2R14 / GOQ / Bitter receptor. / SIGNALING PROTEIN
Function / homology
Function and homology information


bitter taste receptor activity / taste receptor activity / detection of chemical stimulus involved in sensory perception of bitter taste / Class C/3 (Metabotropic glutamate/pheromone receptors) / : / : / : / exo-alpha-sialidase / G protein-coupled receptor activity / Olfactory Signaling Pathway ...bitter taste receptor activity / taste receptor activity / detection of chemical stimulus involved in sensory perception of bitter taste / Class C/3 (Metabotropic glutamate/pheromone receptors) / : / : / : / exo-alpha-sialidase / G protein-coupled receptor activity / Olfactory Signaling Pathway / Activation of the phototransduction cascade / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G protein-coupled acetylcholine receptor signaling pathway / G-protein activation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / Sensory perception of sweet, bitter, and umami (glutamate) taste / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / photoreceptor disc membrane / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / cellular response to catecholamine stimulus / ADORA2B mediated anti-inflammatory cytokines production / sensory perception of taste / ADP signalling through P2Y purinoceptor 1 / 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 / Inactivation, recovery and regulation of the phototransduction cascade / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / extracellular vesicle / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / GTPase binding / retina development in camera-type eye / Ca2+ pathway / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (i) signalling events / fibroblast proliferation / G alpha (s) signalling events / G alpha (q) signalling events / Ras protein signal transduction / cell population proliferation / carbohydrate metabolic process / Extra-nuclear estrogen signaling / G protein-coupled receptor signaling pathway / lysosomal membrane / GTPase activity / synapse / protein-containing complex binding / signal transduction / extracellular exosome / membrane / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Taste receptor type 2 / Taste receptor protein (TAS2R) / BNR repeat-like domain / Glycoside hydrolase, family 33, N-terminal / Trans-sialidase, domain 3 / Sialidase, N-terminal domain / Sialidase family / Sialidase / Sialidase superfamily / G-protein, gamma subunit ...Taste receptor type 2 / Taste receptor protein (TAS2R) / BNR repeat-like domain / Glycoside hydrolase, family 33, N-terminal / Trans-sialidase, domain 3 / Sialidase, N-terminal domain / Sialidase family / Sialidase / Sialidase superfamily / 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 / Guanine nucleotide-binding protein, beta subunit / G-protein, beta subunit / Concanavalin A-like lectin/glucanase domain superfamily / 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. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
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 / exo-alpha-sialidase / Taste receptor type 2 member 14
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.29 Å
AuthorsHu XL / Wu LJ / Hua T / Liu ZJ
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nature / Year: 2024
Title: Bitter taste TAS2R14 activation by intracellular tastants and cholesterol.
Authors: Xiaolong Hu / Weizhen Ao / Mingxin Gao / Lijie Wu / Yuan Pei / Shenhui Liu / Yiran Wu / Fei Zhao / Qianqian Sun / Junlin Liu / Longquan Jiang / Xin Wang / Yan Li / Qiwen Tan / Jie Cheng / ...Authors: Xiaolong Hu / Weizhen Ao / Mingxin Gao / Lijie Wu / Yuan Pei / Shenhui Liu / Yiran Wu / Fei Zhao / Qianqian Sun / Junlin Liu / Longquan Jiang / Xin Wang / Yan Li / Qiwen Tan / Jie Cheng / Fan Yang / Chi Yang / Jinpeng Sun / Tian Hua / Zhi-Jie Liu /
Abstract: Bitter taste receptors, particularly TAS2R14, play central roles in discerning a wide array of bitter substances, ranging from dietary components to pharmaceutical agents. TAS2R14 is also widely ...Bitter taste receptors, particularly TAS2R14, play central roles in discerning a wide array of bitter substances, ranging from dietary components to pharmaceutical agents. TAS2R14 is also widely expressed in extragustatory tissues, suggesting its extra roles in diverse physiological processes and potential therapeutic applications. Here we present cryogenic electron microscopy structures of TAS2R14 in complex with aristolochic acid, flufenamic acid and compound 28.1, coupling with different G-protein subtypes. Uniquely, a cholesterol molecule is observed occupying what is typically an orthosteric site in class A G-protein-coupled receptors. The three potent agonists bind, individually, to the intracellular pockets, suggesting a distinct activation mechanism for this receptor. Comprehensive structural analysis, combined with mutagenesis and molecular dynamic simulation studies, elucidate the broad-spectrum ligand recognition and activation of the receptor by means of intricate multiple ligand-binding sites. Our study also uncovers the specific coupling modes of TAS2R14 with gustducin and G proteins. These findings should be instrumental in advancing knowledge of bitter taste perception and its broader implications in sensory biology and drug discovery.
History
DepositionJan 5, 2024-
Header (metadata) releaseJul 10, 2024-
Map releaseJul 10, 2024-
UpdateNov 6, 2024-
Current statusNov 6, 2024Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_38584.png

Downloads & links

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Map

FileDownload / File: emd_38584.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.04 Å/pix.
x 256 pix.
= 266.24 Å		1.04 Å/pix.
x 256 pix.
= 266.24 Å		1.04 Å/pix.
x 256 pix.
= 266.24 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.04 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02
Minimum - Maximum-0.0025950773 - 1.9139335
Average (Standard dev.)0.0009442536 (±0.022735586)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 266.24 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_38584_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_38584_half_map_2.map
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Sample components

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Entire : Structure of human class T GPCR TAS2R14-Gustducin complex with Ar...

EntireName: Structure of human class T GPCR TAS2R14-Gustducin complex with Aristolochic acid A.
Components
  • Complex: Structure of human class T GPCR TAS2R14-Gustducin complex with Aristolochic acid A.
    • 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: Exo-alpha-sialidase,Taste receptor type 2 member 14,LgBiT
    • Protein or peptide: scFv16
  • Ligand: 8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid
  • Ligand: CHOLESTEROL

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Supramolecule #1: Structure of human class T GPCR TAS2R14-Gustducin complex with Ar...

SupramoleculeName: Structure of human class T GPCR TAS2R14-Gustducin complex with Aristolochic acid A.
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: 42.359008 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDYKDDDDKE NLYFQMGCTL SAEDKAAVER SKMIDRNLQE DAERDARTVK LLLLGAGESG KSTIVKQMKI IHKNGYSEQE CMEFKAVIY SNTLQSILAI VKAMTTLGID YVNPRSAEDQ RQLYAMANTL EDGGMTPQLA EVIKRLWRDP GIQACFERAS E YQLNDSAA ...String:
MDYKDDDDKE NLYFQMGCTL SAEDKAAVER SKMIDRNLQE DAERDARTVK LLLLGAGESG KSTIVKQMKI IHKNGYSEQE CMEFKAVIY SNTLQSILAI VKAMTTLGID YVNPRSAEDQ RQLYAMANTL EDGGMTPQLA EVIKRLWRDP GIQACFERAS E YQLNDSAA YYLNDLDRIT ASGYVPNEQD VLHSRVKTTG IIETQFSFKD LHFRMFDVGG QRSERKKWIH CFEGVTCIIF CA ALSAYDM VLVEDEEVNR MHESLHLFNS ICNHKYFSTT SIVLFLNKKD IFQEKVTKVH LSICFPEYTG PNTFEDAGNY IKN QFLDLN LKKEDKEIYS HMTCATDTQN VKFVFDAVTD IIIKENLKDC GLF

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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: 39.728426 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC RFLDDNQIVT S SGDTTCAL ...String:
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNK VHAIPLRSSW VMTCAYAPSG NYVACGGLDN ICSIYNLKTR EGNVRVSREL AGHTGYLSCC RFLDDNQIVT S SGDTTCAL WDIETGQQTT TFTGHTGDVM SLSLAPDTRL FVSGACDASA KLWDVREGMC RQTFTGHESD INAICFFPNG NA FATGSDD ATCRLFDLRA DQELMTYSHD NIICGITSVS FSKSGRLLLA GYDDFNCNVW DALKADRAGV LAGHDNRVSC LGV TDDGMA VATGSWDSFL KIWNGSSGGG GSGGGGSSGV SGWRLFKKIS

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: Exo-alpha-sialidase,Taste receptor type 2 member 14,LgBiT

MacromoleculeName: Exo-alpha-sialidase,Taste receptor type 2 member 14,LgBiT
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: exo-alpha-sialidase
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 110.840023 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MKTIIALSYI FCLVFADYKD DDDAHHHHHH HHHHENLYFQ SGRAVEGAVK TEPVDLFHPG FLNSSNYRIP ALFKTKEGTL IASIDARRH GGADAPNNDI DTAVRRSEDG GKTWDEGQII MDYPDKSSVI DTTLIQDDET GRIFLLVTHF PSKYGFWNAG L GSGFKNID ...String:
MKTIIALSYI FCLVFADYKD DDDAHHHHHH HHHHENLYFQ SGRAVEGAVK TEPVDLFHPG FLNSSNYRIP ALFKTKEGTL IASIDARRH GGADAPNNDI DTAVRRSEDG GKTWDEGQII MDYPDKSSVI DTTLIQDDET GRIFLLVTHF PSKYGFWNAG L GSGFKNID GKEYLCLYDS SGKEFTVREN VVYDKDSNKT EYTTNALGDL FKNGTKIDNI NSSTAPLKAK GTSYINLVYS DD DGKTWSE PQNINFQVKK DWMKFLGIAP GRGIQIKNGE HKGRIVVPVY YTNEKGKQSS AVIYSDDSGK NWTIGESPND NRK LENGKI INSKTLSDDA PQLTECQVVE MPNGQLKLFM RNLSGYLNIA TSFDGGATWD ETVEKDTNVL EPYCQLSVIN YSQK VDGKD AVIFSNPNAR SRSNGTVRIG LINQVGTYEN GEPKYEFDWK YNKLVKPGYY AYSCLTELSN GNIGLLYEGT PSEEM SYIE MNLKYLESGA NKGSAGSGGV IKSIFTFVLI VEFIIGNLGN SFIALVNCID WVKGRKISSV DRILTALAIS RISLVW LIF GSWCVSVFFP ALFATEKMFR MLTNIWTVIN HFSVWLATGL GTFYFLKIAN FSNSIFLYLK WRVKKVVLVL LLVTSVF LF LNIALINIHI NASINGYRRN KTCSSDSSNF TRFSSLIVLT STVFIFIPFT LSLAMFLLLI FSMWKHRKKM QHTVKISG D ASTKAHRGVK SVITFFLLYA IFSLSFFISV WTSERLEENL IILSQVMGMA YPSCHSCVLI LGNKKLRQAS LSVLLWLRY MFKDGEPSGH KEFRESSGSG SSGSGSSGSG SSVFTLEDFV GDWEQTAAYN LDQVLEQGGV SSLLQNLAVS VTPIQRIVRS GENALKIDI HVIIPYEGLS ADQMAQIEEV FKVVYPVDDH HFKVILPYGT LVIDGVTPNM LNYFGRPYEG IAVFDGKKIT V TGTLWNGN KIIDERLITP DGSMLFRVTI NS

UniProtKB: exo-alpha-sialidase, Taste receptor type 2 member 14

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Macromolecule #5: scFv16

MacromoleculeName: scFv16 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 30.668211 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MVSAIVLYVL LAAAAHSAFA DVQLVESGGG LVQPGGSRKL SCSASGFAFS SFGMHWVRQA PEKGLEWVAY ISSGSGTIYY ADTVKGRFT ISRDDPKNTL FLQMTSLRSE DTAMYYCVRS IYYYGSSPFD FWGQGTTLTV SSGGGGSGGG GSGGGGSDIV M TQATSSVP ...String:
MVSAIVLYVL LAAAAHSAFA DVQLVESGGG LVQPGGSRKL SCSASGFAFS SFGMHWVRQA PEKGLEWVAY ISSGSGTIYY ADTVKGRFT ISRDDPKNTL FLQMTSLRSE DTAMYYCVRS IYYYGSSPFD FWGQGTTLTV SSGGGGSGGG GSGGGGSDIV M TQATSSVP VTPGESVSIS CRSSKSLLHS NGNTYLYWFL QRPGQSPQLL IYRMSNLASG VPDRFSGSGS GTAFTLTISR LE AEDVGVY YCMQHLEYPL TFGAGTKLEL KAAAENLYFQ SHHHHHHHH

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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: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 7 / Number of copies: 1 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL

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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

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.29 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 33406
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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