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TitleMolecular basis for substrate recognition and transport of mammalian taurine transporters.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 27, Page e2425549122, Year 2025
Publish dateJul 8, 2025
AuthorsMingxing Wang / Jin He / Qianwen Cai / Shen-Ao Zhang / Ji She /
PubMed AbstractThe 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.
External linksProc Natl Acad Sci U S A / PubMed:40601627 / PubMed Central
MethodsEM (single particle)
Resolution2.84 - 3.3 Å
Structure data

62434

9kmi

EMDB-62434, PDB-9kmi:
Taurine bound mTAUT
Method: EM (single particle) / Resolution: 3.05 Å

62435

9kmj

EMDB-62435, PDB-9kmj:
Taurine bound hTAUT
Method: EM (single particle) / Resolution: 3.1 Å

62436

9kmk

EMDB-62436, PDB-9kmk:
apo mTAUT in inward open II state
Method: EM (single particle) / Resolution: 3.06 Å

62437

9kml

EMDB-62437, PDB-9kml:
apo mTAUT in inward open I state
Method: EM (single particle) / Resolution: 3.11 Å

62438

9kmm

EMDB-62438, PDB-9kmm:
IAA bound mTAUT
Method: EM (single particle) / Resolution: 3.3 Å

62648

9kyo

EMDB-62648, PDB-9kyo:
GES bound mTAUT
Method: EM (single particle) / Resolution: 2.84 Å

Chemicals

ChemComp-TAU:
2-AMINOETHANESULFONIC ACID

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-IZC:
2H-IMIDAZOL-4-YLACETIC ACID / neurotransmitter*YM

ChemComp-3S5:
Taurocyamine

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / Transporter / Taurine / Chlorine / Sodium / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / SLC6A6

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