Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular basis of human taurine transporter uptake and inhibition.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 7394, Year 2025
Publish date	Aug 11, 2025
Authors	Bowen Du / Lili Cheng / Jiaying Xie / Ligong Chen / Kaige Yan /
PubMed 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.
External links	Nat Commun / PubMed:40789850 / PubMed Central
Methods	EM (single particle)
Resolution	2.92 - 3.45 Å
Structure data	61943 9k0c EMDB-61943, PDB-9k0c: Cryo-EM structural of human taurine transporter TauT in an apo state Method: EM (single particle) / Resolution: 3.06 Å 61948 9k0n EMDB-61948, PDB-9k0n: Cryo-EM structure of human taurine transporter TauT bound with beta-alanine in an occluded state Method: EM (single particle) / Resolution: 3.21 Å 61949 9k0o EMDB-61949, PDB-9k0o: Cryo-EM structure of human taurine transporter TauT bound with GAA in an intermediate state during the transport cycle Method: EM (single particle) / Resolution: 2.95 Å 61970 9k1b EMDB-61970, PDB-9k1b: Cryo-EM structure of human taurine transporter TauT bound with taurine in an occluded state Method: EM (single particle) / Resolution: 3.34 Å 61974 9k1f EMDB-61974, PDB-9k1f: Cryo-EM structure of human taurine transporter TauT bound with GABA in an intermediate conformation in the transport cycle Method: EM (single particle) / Resolution: 3.43 Å 61975 9k1h EMDB-61975, PDB-9k1h: Cryo-EM structure of human taurine transporter TauT bound with P4S in an inward open state Method: EM (single particle) / Resolution: 3.12 Å 61976 9k1i EMDB-61976, PDB-9k1i: Cryo-EM structure of huamn taurine transporter bound with I4AA in inward-open state Method: EM (single particle) / Resolution: 2.92 Å 61981 9k1v EMDB-61981, PDB-9k1v: Cryo-EM structure of human taurine transporter bound with 5AVA in an inward-open state Method: EM (single particle) / Resolution: 2.94 Å 61983 9k1x EMDB-61983, PDB-9k1x: Cryo-EM structure of human taurine transporter TauT bound with GES in an occluded state Method: EM (single particle) / Resolution: 3.06 Å 61985 9k1z EMDB-61985, PDB-9k1z: Cryo-EM structure of human taurine transporter bound with nipecotic acid in an inward open state Method: EM (single particle) / Resolution: 3.27 Å 61987 9k21 EMDB-61987, PDB-9k21: Cryo-EM structure of human taurine transporter TauT bound with homotaurine in an inward-open state Method: EM (single particle) / Resolution: 3.45 Å
Chemicals	ChemComp-CL: Unknown entry ChemComp-BAL: BETA-ALANINE ChemComp-NA: Unknown entry ChemComp-NMG: GUANIDINO ACETATE ChemComp-TAU: 2-AMINOETHANESULFONIC ACID ChemComp-ABU: GAMMA-AMINO-BUTANOIC ACID / neurotransmitter, inhibitorYM PDB-1ebd: DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE ChemComp-IZC: 2H-IMIDAZOL-4-YLACETIC ACID / neurotransmitterYM ChemComp-HOH: WATER ChemComp-KFB: 5-Aminovaleric Acid ChemComp-3S5: Taurocyamine ChemComp-ID7: (3R)-piperidine-3-carboxylic acid ChemComp-A20: 3-aminopropane-1-sulfonic acid
Source	homo sapiens (human)
Keywords	STRUCTURAL PROTEIN/IMMUNE SYSTEM / CL / TRANSPORT PROTEIN / STRUCTURAL PROTEIN-IMMUNE SYSTEM complex / substrate / structural / protein / substrate protein transporter / Inhibitor