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- EMDB-62485: Cryo-EM structure of GPCR16-GiH5 complex -

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Entry
Database: EMDB / ID: EMD-62485
TitleCryo-EM structure of GPCR16-GiH5 complex
Map data
Sample
  • Complex: complex of GPCR with Gigust.
    • Protein or peptide: Guanine nucleotide-binding protein G(i) subunit alpha-1
    • 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: Fusion protein 1,exo-alpha-sialidase,Taste receptor type 2 member 16,Fusion protein 2
    • Protein or peptide: scFv16
  • Ligand: 2-(hydroxymethyl)phenyl beta-D-glucopyranoside
KeywordsGPCR / Complex / SIGNALING PROTEIN
Function / homology
Function and homology information


bitter taste receptor activity / detection of chemical stimulus involved in sensory perception of bitter taste / ganglioside catabolic process / Class C/3 (Metabotropic glutamate/pheromone receptors) / oligosaccharide catabolic process / exo-alpha-sialidase / exo-alpha-sialidase activity / adenylate cyclase inhibitor activity / positive regulation of protein localization to cell cortex / Adenylate cyclase inhibitory pathway ...bitter taste receptor activity / detection of chemical stimulus involved in sensory perception of bitter taste / ganglioside catabolic process / Class C/3 (Metabotropic glutamate/pheromone receptors) / oligosaccharide catabolic process / exo-alpha-sialidase / exo-alpha-sialidase activity / adenylate cyclase inhibitor activity / positive regulation of protein localization to cell cortex / Adenylate cyclase inhibitory pathway / T cell migration / D2 dopamine receptor binding / response to prostaglandin E / adenylate cyclase regulator activity / G protein-coupled serotonin receptor binding / adenylate cyclase-inhibiting serotonin receptor signaling pathway / cellular response to forskolin / regulation of mitotic spindle organization / Regulation of insulin secretion / trans-Golgi network / positive regulation of cholesterol biosynthetic process / negative regulation of insulin secretion / G protein-coupled receptor binding / G protein-coupled receptor activity / response to peptide hormone / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G-protein beta/gamma-subunit complex binding / centriolar satellite / 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 / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / ADP signalling through P2Y purinoceptor 12 / photoreceptor disc membrane / 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 / GDP binding / 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 / Inactivation, recovery and regulation of the phototransduction cascade / cellular response to prostaglandin E stimulus / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / sensory perception of taste / extracellular vesicle / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / retina development in camera-type eye / G protein activity / GTPase binding / Ca2+ pathway / fibroblast proliferation / midbody / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / cell cortex / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Ras protein signal transduction / Extra-nuclear estrogen signaling / cell population proliferation / ciliary basal body / G protein-coupled receptor signaling pathway / lysosomal membrane / cell division / external side of plasma membrane / intracellular membrane-bounded organelle / GTPase activity / synapse / centrosome / GTP binding / protein-containing complex binding / nucleolus / magnesium ion binding / endoplasmic reticulum / Golgi apparatus / signal transduction
Similarity search - Function
: / Taste receptor type 2 / Taste receptor protein (TAS2R) / Glycoside hydrolase, family 33, N-terminal / Trans-sialidase, domain 3 / Sialidase, N-terminal domain / BNR repeat-like domain / Laminin G domain / Laminin G domain / Sialidase family ...: / Taste receptor type 2 / Taste receptor protein (TAS2R) / Glycoside hydrolase, family 33, N-terminal / Trans-sialidase, domain 3 / Sialidase, N-terminal domain / BNR repeat-like domain / Laminin G domain / Laminin G domain / Sialidase family / Sialidase / YSIRK type signal peptide / YSIRK Gram-positive signal peptide / Gram-positive cocci surface proteins LPxTG motif profile. / LPXTG cell wall anchor domain / Sialidase superfamily / G-protein alpha subunit, group I / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / 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 / 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. / 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
Sialidase A / 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 / Guanine nucleotide-binding protein G(i) subunit alpha-1 / Taste receptor type 2 member 16
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.35 Å
AuthorsWang X / Wu LJ / Hua T / Liu ZJ
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of SciencesXDB37030104 China
CitationJournal: Cell Rep / Year: 2025
Title: Structural basis of β-glucopyranoside salicin recognition by a human bitter taste GPCR.
Authors: Xin Wang / Cui Zhou / Weizhen Ao / Lijie Wu / Yiran Wu / Weixiu Xu / Shenhui Liu / Qiwen Tan / Ling Wang / Fei Zhao / Junlin Liu / Yuan Pei / Suwen Zhao / Tian Hua /
Abstract: The human perception of bitterness is mediated by type 2 taste receptors (TAS2Rs), which recognize a broad array of bitter substances with distinct chemical properties. TAS2R16 exhibits a pronounced ...The human perception of bitterness is mediated by type 2 taste receptors (TAS2Rs), which recognize a broad array of bitter substances with distinct chemical properties. TAS2R16 exhibits a pronounced selectivity for β-glucoside-moiety-containing compounds, such as salicin from willow bark. However, the molecular mechanism of moiety-specific recognition and receptor activation in TAS2R16 remains unclear. Here, we present cryoelectron microscopy structures of the salicin-activated human TAS2R16 complexed with gustducin and G and G proteins. The binding mode of salicin with TAS2R16 and the specific interactions of the β-D-glucopyranoside moiety are detailed. Together with molecular docking and mutagenesis data, this study uncovers the structural underpinnings of TAS2R16's group-specific recognition, receptor activation, and subsequent gustducin and G protein coupling. These findings advance our understanding of human bitter taste receptors and provide a foundation for structural modifications of bitter glycosides, opening potential therapeutic applications.
History
DepositionNov 22, 2024-
Header (metadata) releaseApr 2, 2025-
Map releaseApr 2, 2025-
UpdateOct 15, 2025-
Current statusOct 15, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_62485.png

Downloads & links

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Map

FileDownload / File: emd_62485.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: 0.09
Minimum - Maximum-0.001702006 - 1.9550028
Average (Standard dev.)0.0009803051 (±0.022355534)
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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Additional map: #1

Fileemd_62485_additional_1.map
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Half map: #2

Fileemd_62485_half_map_1.map
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Half map: #1

Fileemd_62485_half_map_2.map
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Sample components

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Entire : complex of GPCR with Gigust.

EntireName: complex of GPCR with Gigust.
Components
  • Complex: complex of GPCR with Gigust.
    • Protein or peptide: Guanine nucleotide-binding protein G(i) subunit alpha-1
    • 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: Fusion protein 1,exo-alpha-sialidase,Taste receptor type 2 member 16,Fusion protein 2
    • Protein or peptide: scFv16
  • Ligand: 2-(hydroxymethyl)phenyl beta-D-glucopyranoside

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Supramolecule #1: complex of GPCR with Gigust.

SupramoleculeName: complex of GPCR with Gigust. / 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(i) subunit alpha-1

MacromoleculeName: Guanine nucleotide-binding protein G(i) subunit alpha-1
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 42.191777 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: DYKDDDDKEN LYFQSGCTLS AEDKAAVERS KMIDRNLRED GEKAAREVKL LLLGAGESGK STIVKQMKII HEAGYSEEEC KQYKAVVYS NTIQSIIAII RAMGRLKIDF GDSARADDAR QLFVLAGAAE EGFMTAELAG VIKRLWKDSG VQACFNRSRE Y QLNDSAAY ...String:
DYKDDDDKEN LYFQSGCTLS AEDKAAVERS KMIDRNLRED GEKAAREVKL LLLGAGESGK STIVKQMKII HEAGYSEEEC KQYKAVVYS NTIQSIIAII RAMGRLKIDF GDSARADDAR QLFVLAGAAE EGFMTAELAG VIKRLWKDSG VQACFNRSRE Y QLNDSAAY YLNDLDRIAQ PNYIPTQQDV LRTRVKTTGI VETHFTFKDL HFKMFDVGGQ RSERKKWIHC FEGVTAIIFC VA LSDYDLV LAEDEEMNRM HESMKLFDSI CNNKWFTDTS IILFLNKKDL FEEKIKKSPL TICYPEYAGS NTYEEAAAYI QCQ FEDLNK RKDTKEIYTH FTCATDTQNV KFVFDAVTDI IIKENLKDCG LF

UniProtKB: Guanine nucleotide-binding protein G(i) subunit alpha-1

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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: Fusion protein 1,exo-alpha-sialidase,Taste receptor type 2 member...

MacromoleculeName: Fusion protein 1,exo-alpha-sialidase,Taste receptor type 2 member 16,Fusion protein 2
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: exo-alpha-sialidase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 113.855758 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MKTIIALSYI FCLVFADYKD DDDAHHHHHH HHHHENLYFQ SAHHHHHHSS GLEVLFQGPP EGAALTEKTD IFESGRNGNP NKDGIKSYR IPALLKTDKG TLIAGADERR LHSSDWGDIG MVIRRSEDNG KTWGDRVTIT NLRDNPKASD PSIGSPVNID M VLVQDPET ...String:
MKTIIALSYI FCLVFADYKD DDDAHHHHHH HHHHENLYFQ SAHHHHHHSS GLEVLFQGPP EGAALTEKTD IFESGRNGNP NKDGIKSYR IPALLKTDKG TLIAGADERR LHSSDWGDIG MVIRRSEDNG KTWGDRVTIT NLRDNPKASD PSIGSPVNID M VLVQDPET KRIFSIYDMF PEGKGIFGMS SQKEEAYKKI DGKTYQILYR EGEKGAYTIR ENGTVYTPDG KATDYRVVVD PV KPAYSDK GDLYKGDQLL GNIYFTTNKT SPFRIAKDSY LWMSYSDDDG KTWSAPQDIT PMVKADWMKF LGVGPGTGIV LRN GPHKGR ILIPVYTTNN VSHLDGSQSS RVIYSDDHGK TWHAGEAVND NRQVDGQKIH SSTMNNRRAQ NTESTVVQLN NGDV KLFMR GLTGDLQVAT SKDGGVTWEK DIKRYPQVKD VYVQMSAIHT MHEGKEYIIL SNAGGPKREN GMVHLARVEE NGELT WLKH NPIQKGEFAY NSLQELGNGE YGILYEHTEK GQNAYTLSFR KFNWEFLSKN GSGSGIPIQL TVFFMIIYVL ESLTII VQS SLIVAVLGRE WLQVRRLMPV DMILISLGIS RFCLQWASML NNFCSYFNLN YVLCNLTITW EFFNILTFWL NSLLTVF YC IKVSSFTHHI FLWLRWRILR LFPWILLGCL MITCVTIIPS AIGNYIQIQL LTMEHLPRNS TVTDKLENFH QYQFQAHT V ALVIPFILFL ASTIFLMASL TKQIQHHSTG HCNPSMKARF TALRSLAVLF IVFTSYFLTI LITIIGTLFD KRCWLWVWE AFVYAFILMH STSLMLSSPT LKRILKGKCG SGSGGSGSGG SGSGGSGSGS SGGVFTLEDF VGDWEQTAAY NLDQVLEQGG VSSLLQNLA VSVTPIQRIV RSGENALKID IHVIIPYEGL SADQMAQIEE VFKVVYPVDD HHFKVILPYG TLVIDGVTPN M LNYFGRPY EGIAVFDGKK ITVTGTLWNG NKIIDERLIT PDGSMLFRVT INS

UniProtKB: Sialidase A, Taste receptor type 2 member 16

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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: 28.66682 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 KAAAENLYFQ SHHHHHHHH

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Macromolecule #6: 2-(hydroxymethyl)phenyl beta-D-glucopyranoside

MacromoleculeName: 2-(hydroxymethyl)phenyl beta-D-glucopyranoside / type: ligand / ID: 6 / Number of copies: 1 / Formula: SA0
Molecular weightTheoretical: 286.278 Da
Chemical component information

ChemComp-SA0:
2-(hydroxymethyl)phenyl beta-D-glucopyranoside

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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

MicroscopeTFS 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

CTF correctionType: NONE
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.35 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 103932
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9kpe:
Cryo-EM structure of GPCR16-GiH5 complex

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