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- EMDB-49613: Local refinement map of the human sweet taste receptor Venus Fly ... -

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Basic information

Entry
Database: EMDB / ID: EMD-49613
TitleLocal refinement map of the human sweet taste receptor Venus Fly Trap domains (VFT) and upper-half of the Cysteine-Rich domains (CR) from the sucralose dataset
Map data
Sample
  • Complex: Local refinement map of the human sweet taste receptor Venus Fly Trap domains (VFT) and upper-half of the Cysteine-Rich domains (CR) from the sucralose dataset
KeywordsSweet / taste / receptor / GPCR / TAS1R2 / TAS1R3 / T1R2 / T1R3 / MEMBRANE PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsJuen Z / Lu Z / Yu R / Chang AN / Wang B / Fitzpatrick AWP / Zuker CS
Funding support United States, 1 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Cell / Year: 2025
Title: The structure of human sweetness.
Authors: Zhang Juen / Zhengyuan Lu / Ruihuan Yu / Andrew N Chang / Brian Wang / Anthony W P Fitzpatrick / Charles S Zuker /
Abstract: In humans, the detection and ultimately the perception of sweetness begin in the oral cavity, where taste receptor cells (TRCs) dedicated to sweet-sensing interact with sugars, artificial sweeteners, ...In humans, the detection and ultimately the perception of sweetness begin in the oral cavity, where taste receptor cells (TRCs) dedicated to sweet-sensing interact with sugars, artificial sweeteners, and other sweet-tasting chemicals. Human sweet TRCs express on their cell surface a sweet receptor that initiates the cascade of signaling events responsible for our strong attraction to sweet stimuli. Here, we describe the cryo-electron microscopy (cryo-EM) structure of the human sweet receptor bound to two of the most widely used artificial sweeteners-sucralose and aspartame. Our results reveal the structural basis for sweet detection, provide insights into how a single receptor mediates all our responses to such a wide range of sweet-tasting compounds, and open up unique possibilities for designing a generation of taste modulators informed by the structure of the human receptor.
History
DepositionMar 10, 2025-
Header (metadata) releaseMay 14, 2025-
Map releaseMay 14, 2025-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_49613.png

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Map

FileDownload / File: emd_49613.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 440 pix.
= 362.12 Å		0.82 Å/pix.
x 440 pix.
= 362.12 Å		0.82 Å/pix.
x 440 pix.
= 362.12 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.823 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.47
Minimum - Maximum-1.8080275 - 2.8853729
Average (Standard dev.)-0.000106930325 (±0.0481407)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 362.12 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_49613_half_map_1.map
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Half map: #2

Fileemd_49613_half_map_2.map
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Sample components

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Entire : Local refinement map of the human sweet taste receptor Venus Fly ...

EntireName: Local refinement map of the human sweet taste receptor Venus Fly Trap domains (VFT) and upper-half of the Cysteine-Rich domains (CR) from the sucralose dataset
Components
  • Complex: Local refinement map of the human sweet taste receptor Venus Fly Trap domains (VFT) and upper-half of the Cysteine-Rich domains (CR) from the sucralose dataset

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Supramolecule #1: Local refinement map of the human sweet taste receptor Venus Fly ...

SupramoleculeName: Local refinement map of the human sweet taste receptor Venus Fly Trap domains (VFT) and upper-half of the Cysteine-Rich domains (CR) from the sucralose dataset
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)

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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: 59.0 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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 114542
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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