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- EMDB-62738: Structure of human apo Taurine Transporter in the inward-open con... -

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Basic information

Entry
Database: EMDB / ID: EMD-62738
TitleStructure of human apo Taurine Transporter in the inward-open conformation
Map data
Sample
  • Complex: TAUT
    • Protein or peptide: Sodium- and chloride-dependent taurine transporter
  • Ligand: CHOLESTEROL HEMISUCCINATE
Keywordscancer / TRANSPORT PROTEIN
Function / homology
Function and homology information


taurine transmembrane transporter activity / alanine transmembrane transporter activity / gamma-aminobutyric acid transmembrane transporter activity / taurine:sodium symporter activity / import across plasma membrane / gamma-aminobutyric acid import / gamma-aminobutyric acid:sodium:chloride symporter activity / alanine transport / amino acid:sodium symporter activity / taurine transmembrane transport ...taurine transmembrane transporter activity / alanine transmembrane transporter activity / gamma-aminobutyric acid transmembrane transporter activity / taurine:sodium symporter activity / import across plasma membrane / gamma-aminobutyric acid import / gamma-aminobutyric acid:sodium:chloride symporter activity / alanine transport / amino acid:sodium symporter activity / taurine transmembrane transport / amino acid import across plasma membrane / Amino acid transport across the plasma membrane / amino acid transmembrane transporter activity / SLC-mediated transport of neurotransmitters / microvillus membrane / neurotransmitter transport / amino acid transport / transport across blood-brain barrier / cell projection / sodium ion transmembrane transport / positive regulation of cell differentiation / modulation of chemical synaptic transmission / GABA-ergic synapse / basolateral plasma membrane / postsynaptic membrane / apical plasma membrane / neuronal cell body / dendrite / 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 speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.33 Å
AuthorsWu JX / Qi Y
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32371266 China
CitationJournal: Nat Commun / Year: 2026
Title: Structural mechanism of substrate binding and inhibition of human taurine transporter.
Authors: Yuhan Qi / Ying Zhang / Duanning Wang / Jiameng Liu / Yue Zhou / Wenming Ji / Xinjing Chen / Luping Liu / Rui Wang / Jing-Xiang Wu /
Abstract: Taurine is a sulfur-containing amino acid that plays several crucial roles in the body. Its uptake is mediated by the taurine transporter (TauT). Genetic mutations and dysregulation of TauT have been ...Taurine is a sulfur-containing amino acid that plays several crucial roles in the body. Its uptake is mediated by the taurine transporter (TauT). Genetic mutations and dysregulation of TauT have been linked to various neurological disorders, cardiomyopathy, childhood progressive retinal degeneration, and cancer, making TauT a promising target for therapeutic intervention in these diseases. However, the structure and mechanism of TauT remain poorly understood. In this study, we present the structures of the human taurine transporter (hTauT) under four conditions: the substrate-free state, the taurine-bound state, the β-alanine-bound state, and the cyclic inhibitor piperidine-4-sulfonate (P4S)-bound state. These structures reveal that taurine binds at the central substrate-binding site of hTauT. Notably, β-alanine and the cyclic P4S inhibitors also mimic taurine, occupying the same substrate-binding site. In the substrate-free and P4S-bound forms, hTauT also adopt an inward-open conformation, where transmembrane helix TM1a bends toward the membrane, facilitating the opening of the intracellular gate for ion and substrate release. These structural insights enhance our understanding of the mechanisms underlying substrate and ion recognition and transport in hTauT, paving the way for the future development of taurine transporter substrate analogues or selective inhibitors.
History
DepositionDec 14, 2024-
Header (metadata) releaseApr 15, 2026-
Map releaseApr 15, 2026-
UpdateApr 15, 2026-
Current statusApr 15, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_62738.png

Downloads & links

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Map

FileDownload / File: emd_62738.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.)
1.07 Å/pix.
x 256 pix.
= 273.152 Å		1.07 Å/pix.
x 256 pix.
= 273.152 Å		1.07 Å/pix.
x 256 pix.
= 273.152 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.067 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.35
Minimum - Maximum-2.1157072 - 3.2409608
Average (Standard dev.)-0.0042017694 (±0.067993134)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 273.152 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_62738_msk_1.map
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Half map: #2

Fileemd_62738_half_map_1.map
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Half map: #1

Fileemd_62738_half_map_2.map
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Sample components

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Entire : TAUT

EntireName: TAUT
Components
  • Complex: TAUT
    • Protein or peptide: Sodium- and chloride-dependent taurine transporter
  • Ligand: CHOLESTEROL HEMISUCCINATE

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Supramolecule #1: TAUT

SupramoleculeName: TAUT / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Sodium- and chloride-dependent taurine transporter

MacromoleculeName: Sodium- and chloride-dependent taurine transporter / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 69.881633 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEAEGKPPQ REKWSSKIDF VLSVAGGFVG LGNVWRFPYL CYKNGGGAFL IPYFIFLFG SGLPVFFLEI IIGQYTSEGG ITCWEKICPL FSGIGYASVV IVSLLNVYYI VILAWATYYL FQSFQKELPW A HCNHSWNT ...String:
MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEAEGKPPQ REKWSSKIDF VLSVAGGFVG LGNVWRFPYL CYKNGGGAFL IPYFIFLFG SGLPVFFLEI IIGQYTSEGG ITCWEKICPL FSGIGYASVV IVSLLNVYYI VILAWATYYL FQSFQKELPW A HCNHSWNT PHCMEDTMRK NKSVWITISS TNFTSPVIEF WERNVLSLSP GIDHPGSLKW DLALCLLLVW LVCFFCIWKG VR STGKVVY FTATFPFAML LVLLVRGLTL PGAGAGIKFY LYPDITRLED PQVWIDAGTQ IFFSYAICLG AMTSLGSYNK YKY NSYRDC MLLGCLNSGT SFVSGFAIFS ILGFMAQEQG VDIADVAESG PGLAFIAYPK AVTMMPLPTF WSILFFIMLL LLGL DSQFV EVEGQITSLV DLYPSFLRKG YRREIFIAFV CSISYLLGLT MVTEGGMYVF QLFDYYAASG VCLLWVAFFE CFVIA WIYG GDNLYDGIED MIGYRPGPWM KYSWAVITPV LCVGCFIFSL VKYVPLTYNK TYVYPNWAIG LGWSLALSSM LCVPLV IVI RLCQTEGPFL VRVKYLLTPR EPNRWAVERE GATPYNSRTV MNGALVKPTH IIVETMM

UniProtKB: Sodium- and chloride-dependent taurine transporter

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Macromolecule #2: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 2 / Number of copies: 1 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated magnification: 81000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.33 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: Coot / Number images used: 80335
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER
FSC plot (resolution estimation)

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