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- EMDB-62648: GES bound mTAUT -

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Basic information

Entry
Database: EMDB / ID: EMD-62648
TitleGES bound mTAUT
Map data
Sample
  • Complex: GES bound mTAUT
    • Protein or peptide: Heavy chain of 9D5 fab
    • Protein or peptide: Sodium- and chloride-dependent taurine transporter
    • Protein or peptide: Light chain of 9D5 fab
  • Ligand: SODIUM ION
  • Ligand: CHLORIDE ION
  • Ligand: Taurocyamine
  • Ligand: water
KeywordsTaurine / transporter / SLC6A6 / MEMBRANE PROTEIN/IMMUNE SYSTEM / MEMBRANE PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


SLC-mediated transport of neurotransmitters / Amino acid transport across the plasma membrane / alanine transmembrane transporter activity / taurine:sodium symporter activity / gamma-aminobutyric acid:sodium:chloride symporter activity / amino acid:sodium symporter activity / amino acid import across plasma membrane / taurine transmembrane transport / neurotransmitter transport / microvillus membrane ...SLC-mediated transport of neurotransmitters / Amino acid transport across the plasma membrane / alanine transmembrane transporter activity / taurine:sodium symporter activity / gamma-aminobutyric acid:sodium:chloride symporter activity / amino acid:sodium symporter activity / amino acid import across plasma membrane / taurine transmembrane transport / neurotransmitter transport / microvillus membrane / positive regulation of cell differentiation / modulation of chemical synaptic transmission / GABA-ergic synapse / basolateral plasma membrane / postsynaptic membrane / apical plasma membrane / plasma membrane
Similarity search - Function
Sodium:neurotransmitter symporter, taurine / Sodium:neurotransmitter symporter family signature 2. / Sodium:neurotransmitter symporter family signature 1. / Sodium:neurotransmitter symporter / Sodium:neurotransmitter symporter superfamily / Sodium:neurotransmitter symporter family / Sodium:neurotransmitter symporter family profile.
Similarity search - Domain/homology
Sodium- and chloride-dependent taurine transporter
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.84 Å
AuthorsShe J / Wang MX / He J
Funding support China, 4 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2021YFF0600801 China
National Natural Science Foundation of China (NSFC)32071201 China
National Natural Science Foundation of China (NSFC)32100967 China
The Center for Advanced Interdisciplinary Science and Biomedicine of IHMQYPY20220009 China
CitationJournal: Proc Natl Acad Sci U S A / Year: 2025
Title: Molecular basis for substrate recognition and transport of mammalian taurine transporters.
Authors: Mingxing Wang / Jin He / Qianwen Cai / Shen-Ao Zhang / Ji She /
Abstract: The taurine transporter (TAUT) mediates cellular taurine uptake, playing a critical role in human health and longevity. In this study, we present cryogenic electron microscopy structures of both ...The taurine transporter (TAUT) mediates cellular taurine uptake, playing a critical role in human health and longevity. In this study, we present cryogenic electron microscopy structures of both mouse and human TAUT in various conformational states. The taurine-bound, occluded forms of mouse and human TAUT reveal the substrate binding pocket and the ion binding sites. The amino group of taurine interacts with Glu406 at the binding site, constituting a key structural feature determining substrate preference. While both imidazole acetic acid and guanidinoethyl sulfonate (GES) inhibit TAUT by competing with taurine for the binding site, GES also functions as a substrate of TAUT. Moreover, mouse TAUT is captured in an inward-open apo conformation, where the tilted movement of transmembrane helix (TM) 1a opens the intracellular gate. Notably, TM6 exhibits two distinct conformational states: the canonical form consisting of two half-helices and a continuous straight helix. In the latter conformation, TM6 partially occupies the substrate binding site, likely promoting taurine release. Together, our findings provide critical insights into the molecular mechanisms by which TAUT recognizes and transports taurine.
History
DepositionDec 9, 2024-
Header (metadata) releaseJul 2, 2025-
Map releaseJul 2, 2025-
UpdateJul 16, 2025-
Current statusJul 16, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_62648.png

Downloads & links

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Map

FileDownload / File: emd_62648.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 384 pix.
= 314.88 Å		0.82 Å/pix.
x 384 pix.
= 314.88 Å		0.82 Å/pix.
x 384 pix.
= 314.88 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-1.3804353 - 2.1504834
Average (Standard dev.)-0.00032928132 (±0.03036689)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 314.88 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_62648_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_62648_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : GES bound mTAUT

EntireName: GES bound mTAUT
Components
  • Complex: GES bound mTAUT
    • Protein or peptide: Heavy chain of 9D5 fab
    • Protein or peptide: Sodium- and chloride-dependent taurine transporter
    • Protein or peptide: Light chain of 9D5 fab
  • Ligand: SODIUM ION
  • Ligand: CHLORIDE ION
  • Ligand: Taurocyamine
  • Ligand: water

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Supramolecule #1: GES bound mTAUT

SupramoleculeName: GES bound mTAUT / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Heavy chain of 9D5 fab

MacromoleculeName: Heavy chain of 9D5 fab / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 13.138654 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
EVQLVESGGG LVKPGGSLKL SCAASGFTFS SYAMSWVRQS PEKRLEWVAE ISSGGRYIYY SDTVTGRFTI SRDNARNILH LEMSSLRSE DTAMYYCARG EVRQRGFDYW GQGTTLTVS

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Macromolecule #2: Sodium- and chloride-dependent taurine transporter

MacromoleculeName: Sodium- and chloride-dependent taurine transporter / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 70.051891 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEADGKPPQ REKWSSKIDF VLSVAGGFVG LGNVWRFPYL CYKNGGGAFL IPYFIFLFG SGLPVFFLEV IIGQYTSEGG ITCWEKICPL FSGIGYASIV IVSLLNVYYI VILAWATYYL FHSFQKDLPW A HCNHSWNT ...String:
MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEADGKPPQ REKWSSKIDF VLSVAGGFVG LGNVWRFPYL CYKNGGGAFL IPYFIFLFG SGLPVFFLEV IIGQYTSEGG ITCWEKICPL FSGIGYASIV IVSLLNVYYI VILAWATYYL FHSFQKDLPW A HCNHSWNT PQCMEDTLRR NESHWVSLST ANFTSPVIEF WERNVLSLSS GIDNPGSLKW DLALCLLLVW LVCFFCIWKG VR STGKVVY FTATFPFAML LVLLVRGLTL PGAGEGIKFY LYPDISRLGD PQVWIDAGTQ IFFSYAICLG AMTSLGSYNK YKY NSYRDC MLLGCLNSGT SFVSGFAIFS ILGFMAQEQG VDIADVAESG PGLAFIAYPK AVTMMPLPTF WSILFFIMLL LLGL DSQFV EVEGQITSLV DLYPSFLRKG YRREIFIAIL CSISYLLGLT MVTEGGMYVF QLFDYYAASG VCLLWVAFFE CFVIA WIYG VNRFSEDIRD MIGYRPGPWM KYSWAVITPA LCVGCFVFSL VKYVPLTYNK VYRYPDWAIG LGWGLALSSM LCIPLV IVI LLCRTEGPLR VRIKYLITPR EPNRWAVERE GATPFHSRVT LMNGALMKPS HVIVETMM

UniProtKB: Sodium- and chloride-dependent taurine transporter

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Macromolecule #3: Light chain of 9D5 fab

MacromoleculeName: Light chain of 9D5 fab / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 11.480681 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
ENVLTQSPAI MSTSPGEKVT MTCRASSSVG SSYLHWYQQK SGASPKLWIY STSNLASGVP ARFSGSGSGT SYSLTISSVE AEDAATYYC QQFSGYPLTF GSGTKLEMK

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Macromolecule #4: SODIUM ION

MacromoleculeName: SODIUM ION / type: ligand / ID: 4 / Number of copies: 2
Molecular weightTheoretical: 22.99 Da

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Macromolecule #5: CHLORIDE ION

MacromoleculeName: CHLORIDE ION / type: ligand / ID: 5 / Number of copies: 1 / Formula: CL
Molecular weightTheoretical: 35.453 Da

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Macromolecule #6: Taurocyamine

MacromoleculeName: Taurocyamine / type: ligand / ID: 6 / Number of copies: 1 / Formula: 3S5
Molecular weightTheoretical: 167.187 Da
Chemical component information

ChemComp-3S5:
Taurocyamine

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Macromolecule #7: water

MacromoleculeName: water / type: ligand / ID: 7 / Number of copies: 1 / 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

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 54.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.7 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.84 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 266435
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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