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- EMDB-61987: Cryo-EM structure of human taurine transporter TauT bound with ho... -

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Basic information

Entry
Database: EMDB / ID: EMD-61987
TitleCryo-EM structure of human taurine transporter TauT bound with homotaurine in an inward-open state
Map data
Sample
  • Complex: Human taurine transporter complex with homotaurine in an inward-open state
    • Protein or peptide: Fragment antigen binding heavy chain
    • Protein or peptide: Fragment antigen binding light chain
    • Protein or peptide: Sodium- and chloride-dependent taurine transporter
  • Ligand: CHLORIDE ION
  • Ligand: 3-aminopropane-1-sulfonic acid
KeywordsInhibitor / transport protein / structural / STRUCTURAL PROTEIN/IMMUNE SYSTEM / STRUCTURAL PROTEIN-IMMUNE SYSTEM complex
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 / amino acid import across plasma membrane ...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 / amino acid import across plasma membrane / taurine transmembrane transport / Amino acid transport across the plasma membrane / amino acid transmembrane transporter activity / SLC-mediated transport of neurotransmitters / neurotransmitter transport / microvillus membrane / amino acid transport / transport across blood-brain barrier / sodium ion transmembrane transport / cell projection / 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: 3.45 Å
AuthorsDu B / Yan K
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Nat Commun / Year: 2025
Title: Molecular basis of human taurine transporter uptake and inhibition.
Authors: Bowen Du / Lili Cheng / Jiaying Xie / Ligong Chen / Kaige Yan /
Abstract: The taurine transporter, TauT, regulates various taurine-mediated physiological and pathological functions by facilitating taurine uptake in a sodium- and chloride-dependent manner. Dysfunction of ...The taurine transporter, TauT, regulates various taurine-mediated physiological and pathological functions by facilitating taurine uptake in a sodium- and chloride-dependent manner. Dysfunction of TauT is associated with male infertility, retinal health and cancers. Despite extensive research efforts, the intricate structure of TauT, the molecular mechanisms underlying taurine transport, and the inhibition mechanisms involved, all remain elusive. Here, we present eleven cryo-electron microscopy (cryo-EM) structures of TauT. The structures TauT bound to substrate (taurine) and substrate analogues (β-alanine, guanidinoacetate, and γ-aminobutyric acid), are captured in distinct conformations. Combining with biochemical analyses, these structures reveal that amino acids Leu134 and Glu406 play a crucial role in substrate specificity within the GABA subfamily. Five distinct inhibitors, namely, piperidine-4-sulfonic acid, imidazole-4-acetatic acid, 5-aminovaleric acid, nipecotic acid and homotaurine, stabilize TauT in an inward-open conformation. Conversely, guanidinoethyl sulphonate stabilizes TauT in the occluded state. These structural insights offer a comprehensive understanding of how these inhibitors counteract taurine transport. Collectively, these findings advance our understanding of the substrate coordination and inhibitor recognition mechanisms of TauT.
History
DepositionOct 16, 2024-
Header (metadata) releaseAug 20, 2025-
Map releaseAug 20, 2025-
UpdateSep 10, 2025-
Current statusSep 10, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_61987.png

Downloads & links

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Map

FileDownload / File: emd_61987.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 256 pix.
= 274.432 Å		1.07 Å/pix.
x 256 pix.
= 274.432 Å		1.07 Å/pix.
x 256 pix.
= 274.432 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.072 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.4
Minimum - Maximum-2.0404572 - 3.003456
Average (Standard dev.)-0.0026788868 (±0.06512667)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 274.432 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_61987_half_map_1.map
Projections & Slices
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Slices (1/2)
Density Histograms

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Histogram (log scale)

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Half map: #1

Fileemd_61987_half_map_2.map
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Sample components

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Entire : Human taurine transporter complex with homotaurine in an inward-o...

EntireName: Human taurine transporter complex with homotaurine in an inward-open state
Components
  • Complex: Human taurine transporter complex with homotaurine in an inward-open state
    • Protein or peptide: Fragment antigen binding heavy chain
    • Protein or peptide: Fragment antigen binding light chain
    • Protein or peptide: Sodium- and chloride-dependent taurine transporter
  • Ligand: CHLORIDE ION
  • Ligand: 3-aminopropane-1-sulfonic acid

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Supramolecule #1: Human taurine transporter complex with homotaurine in an inward-o...

SupramoleculeName: Human taurine transporter complex with homotaurine in an inward-open state
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Fragment antigen binding heavy chain

MacromoleculeName: Fragment antigen binding heavy chain / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.138654 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
EVQLVESGGG LVKPGGSLKL SCAASGFTFS SYAMSWVRQS PEKRLEWVAE ISSGGRYIYY SDTVTGRFTI SRDNARNILH LEMSSLRSE DTAMYYCARG EVRQRGFDYW GQGTTLTVS

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Macromolecule #2: Fragment antigen binding light chain

MacromoleculeName: Fragment antigen binding light chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.920076 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
ENVLTQSPAI MSTSPGEKVT MTCRASSSVG SSYLHWYQQK SGASPKLWIY STSNLASGVP ARFSGSGSGT SYSLTISSVE AEDAATYYC QQFSGYPLTF GSGTKLEMGS DEVDAGSHHH HHHHHHHGSV EDYKDDDDK

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Macromolecule #3: Sodium- and chloride-dependent taurine transporter

MacromoleculeName: Sodium- and chloride-dependent taurine transporter / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 73.446273 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 YHN NVYRDC MLLGCLNSGT SFVSGFAIFS ILGFMAQEQG VDIADVAESG PGLAFIAYPK AVTMMPLPTF WSILFFIMLL LLGL DSQFV EVEGQITSLV DLYPSFLRKG YRREIFIAFV CSISYLLGLT MVTEGGMYVF QLFDYYAASG VCLLWVAFFE CFVIA WIYG GNRFSEDIRD MIGFPPGPWM KYSWAVITPV LCVGCFIFSL VKYVPLTYNK TYVYPNWAIG LGWSLALSSM LCVPLV IVI RLCQTEGPFL VRVKYLLTPR EPNRWAVERE GATPYNSRTV MNGALVKPTH IIVETMMGSD EVDAGSHHHH HHHHHHG SV EDYKDDDDK

UniProtKB: Sodium- and chloride-dependent taurine transporter

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Macromolecule #4: CHLORIDE ION

MacromoleculeName: CHLORIDE ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: CL
Molecular weightTheoretical: 35.453 Da

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Macromolecule #5: 3-aminopropane-1-sulfonic acid

MacromoleculeName: 3-aminopropane-1-sulfonic acid / type: ligand / ID: 5 / Number of copies: 1 / Formula: A20
Molecular weightTheoretical: 139.173 Da
Chemical component information

ChemComp-A20:
3-aminopropane-1-sulfonic acid

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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

MicroscopeFEI POLARA 300
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / 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: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.45 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 164725
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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