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Structural insights into a conserved mechanism of choline translocation through CHT - PubMed

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  • #choline transporter
  • #cryo-EM structure
  • #evolutionary conservation
  • Choline is an essential nutrient for cellular homeostasis in all organisms.
  • Human cholinergic neurons use high-affinity Na+-dependent transporter SLC5A7 (CHT1) for choline uptake.
  • Bacteria also rely on choline for osmo-protection and metabolism, suggesting similar transporters.
  • A bacterial Na+-dependent choline transporter (sfCHT) with high sequence identity to CHT1 was identified and characterized.
  • Cryo-EM structures show sfCHT has a LeuT-fold architecture and similar Na+ coordination to CHT1.
  • sfCHT was captured in an inward-facing conformation with choline near the cytoplasmic side.
  • Computational analysis and transport assays revealed conserved residues and conformational rearrangements.
  • The findings suggest an evolutionarily conserved mechanism for choline translocation in bacterial and human transporters.