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- EMDB-70736: Structure of the sweet receptor bound to advantame in the compact... -

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Basic information

Entry
Database: EMDB / ID: EMD-70736
TitleStructure of the sweet receptor bound to advantame in the compact state, transmembrane domain
Map data
Sample
  • Complex: Human TAS1R2 and mouse TAS1R3 sweet receptor bound to advantame
    • Complex: TAS1R2
    • Complex: TAS1R3
KeywordsMembrane protein / GPCR / SIGNALING PROTEIN
Biological speciesHomo sapiens (human) / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsWang H / Chen X / Dai Y / Lee CH
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM143282 United States
CitationJournal: Cell Res / Year: 2025
Title: Structure and activation mechanism of human sweet taste receptor.
Authors: Haolan Wang / Xiao Chen / Yaxin Dai / Shabareesh Pidathala / Yiming Niu / Chen Zhao / Siyu Li / Liang Wang / Chia-Hsueh Lee /
History
DepositionMay 20, 2025-
Header (metadata) releaseSep 3, 2025-
Map releaseSep 3, 2025-
UpdateNov 19, 2025-
Current statusNov 19, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_70736.png

Downloads & links

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Map

FileDownload / File: emd_70736.map.gz / Format: CCP4 / Size: 38.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.44 Å/pix.
x 216 pix.
= 311.515 Å		1.44 Å/pix.
x 216 pix.
= 311.515 Å		1.44 Å/pix.
x 216 pix.
= 311.515 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.4422 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.875
Minimum - Maximum-2.3444364 - 3.8104994
Average (Standard dev.)0.0049430532 (±0.07841987)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions216216216
Spacing216216216
CellA=B=C: 311.5152 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_70736_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_70736_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human TAS1R2 and mouse TAS1R3 sweet receptor bound to advantame

EntireName: Human TAS1R2 and mouse TAS1R3 sweet receptor bound to advantame
Components
  • Complex: Human TAS1R2 and mouse TAS1R3 sweet receptor bound to advantame
    • Complex: TAS1R2
    • Complex: TAS1R3

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Supramolecule #1: Human TAS1R2 and mouse TAS1R3 sweet receptor bound to advantame

SupramoleculeName: Human TAS1R2 and mouse TAS1R3 sweet receptor bound to advantame
type: complex / ID: 1 / Parent: 0

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Supramolecule #2: TAS1R2

SupramoleculeName: TAS1R2 / type: complex / ID: 2 / Parent: 1
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: TAS1R3

SupramoleculeName: TAS1R3 / type: complex / ID: 3 / Parent: 1
Source (natural)Organism: Mus musculus (house mouse)

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.1 µm / Nominal defocus min: 1.1 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 140239
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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