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- PDB-9kmj: Taurine bound hTAUT -

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Basic information

Entry
Database: PDB / ID: 9kmj
TitleTaurine bound hTAUT
Components
  • Heavy chain of 9D5 Fab
  • Light chain of 9D5 Fab
  • Sodium- and chloride-dependent taurine transporter
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / Transporter / Taurine / Chlorine / Sodium / MEMBRANE 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
2-AMINOETHANESULFONIC ACID / Sodium- and chloride-dependent taurine transporter
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsShe, J. / Wang, M. / He, J.
Funding support China, 4items
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
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
DepositionNov 16, 2024Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 2, 2025Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 2, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Jul 16, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
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Revision 1.2Jul 23, 2025Group: Data collection / Category: em_admin / em_software / Item: _em_admin.last_update / _em_software.name
Revision 1.1Jul 23, 2025Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Data processing / Experimental summary / Data content type: EM metadata / EM metadata / Category: em_admin / em_software / Data content type: EM metadata / EM metadata / Item: _em_admin.last_update / _em_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Sodium- and chloride-dependent taurine transporter
H: Heavy chain of 9D5 Fab
L: Light chain of 9D5 Fab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,8507
Polymers94,6433
Non-polymers2074
Water181
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Sodium- and chloride-dependent taurine transporter / Solute carrier family 6 member 6


Mass: 70023.891 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC6A6 / Production host: Homo sapiens (human) / References: UniProt: P31641

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Antibody , 2 types, 2 molecules HL

#2: Antibody Heavy chain of 9D5 Fab


Mass: 13138.654 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Spodoptera frugiperda (fall armyworm)
#3: Antibody Light chain of 9D5 Fab


Mass: 11480.681 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Spodoptera frugiperda (fall armyworm)

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Non-polymers , 4 types, 5 molecules

#4: Chemical ChemComp-TAU / 2-AMINOETHANESULFONIC ACID


Mass: 125.147 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H7NO3S / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Taurine bound hTAUT / Type: COMPLEX / Entity ID: #2, #1, #3 / Source: MULTIPLE SOURCES
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2700 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 54 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: NONE
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 324787 / Symmetry type: POINT
RefinementStereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0066193
ELECTRON MICROSCOPYf_angle_d0.8368422
ELECTRON MICROSCOPYf_dihedral_angle_d8.443835
ELECTRON MICROSCOPYf_chiral_restr0.052920
ELECTRON MICROSCOPYf_plane_restr0.0071036

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