9RWT
high-affinity choline transporter in DDM with Na+
Summary for 9RWT
| Entry DOI | 10.2210/pdb9rwt/pdb |
| EMDB information | 54346 54347 |
| Descriptor | Solute carrier family 5 (High affinity choline transporter), member 7, SODIUM ION (2 entities in total) |
| Functional Keywords | choline transporter, membrane protein |
| Biological source | Salimicrobium flavidum |
| Total number of polymer chains | 1 |
| Total formula weight | 59729.90 |
| Authors | Vilchez-Garcia, J.,Lopez-Alonso, J.P.,Jiang, H.,Ubarretxena-Belandia, I.,Tascon, I. (deposition date: 2025-07-10, release date: 2026-04-29, Last modification date: 2026-06-10) |
| Primary citation | Vilchez-Garcia, J.,Martinez-Jimenez, A.,Jiang, H.,Luengo, M.,Ochoa-Lizarralde, B.,Lopez-Alonso, J.P.,Perez-Lorente, J.,Bartoccioni, P.,Estevez, R.,Guallar, V.,Errasti-Murugarren, E.,Ubarretxena-Belandia, I.,Tascon, I. Structural insights into a conserved mechanism of choline translocation through CHT. Sci Adv, 12:eaec1241-eaec1241, 2026 Cited by PubMed Abstract: Choline is an essential nutrient critical for cellular homeostasis across all domains of life. In humans, choline uptake in cholinergic neurons for its recycling into acetylcholine is mediated by the high-affinity Na-dependent transporter SLC5A7 (CHT1). Prokaryotes also depend on choline as an osmo-protectant and as metabolite, raising the possibility that bacteria also have choline transporters akin to CHT1. Here, we identify and characterize a bacterial Na-dependent choline transporter (sfCHT) with high sequence identity to CHT1. Cryo-EM structures of Na- and choline-bound sfCHT reveal a LeuT-fold architecture with Na coordination geometry similar to CHT1. Captured in an inward-facing conformation, in sfCHT choline is found at a site near the cytoplasmic side. Computational analysis and transport assays of sfCHT and CHT1 variants reveal local conformational rearrangements in conserved residues along a defined pathway to the cytosolic site. These findings provide structural and mechanistic insights into intracellular choline transition, suggesting an evolutionarily conserved mechanism between the bacterial and human choline transporters. PubMed: 42213839DOI: 10.1126/sciadv.aec1241 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.83 Å) |
Structure validation
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