Structural highlights
Function
S23A1_MOUSE Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.[UniProtKB:Q9UHI7]
Publication Abstract from PubMed
Vitamin C (L-ascorbic acid) is an essential nutrient for human health, and its deficiency has long been known to cause scurvy. Sodium-dependent vitamin C transporters (SVCTs) are responsible for vitamin C uptake and tissue distribution in mammals. Here, we present cryogenic electron microscopy structures of mouse SVCT1 in both the apo and substrate-bound states. Mouse SVCT1 forms a homodimer with each protomer containing a core domain and a gate domain. The tightly packed extracellular interfaces between the core domain and gate domain stabilize the protein in an inward-open conformation for both the apo and substrate-bound structures. Vitamin C binds at the core domain of each subunit, and two potential sodium ions are identified near the binding site. The coordination of sodium ions by vitamin C explains their coupling transport. SVCTs probably deliver substrate through an elevator mechanism in combination with local structural arrangements. Altogether, our results reveal the molecular mechanism by which SVCTs recognize vitamin C and lay a foundation for further mechanistic studies on SVCT substrate transport.
Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter.,Wang M, He J, Li S, Cai Q, Zhang K, She J Nat Commun. 2023 Mar 13;14(1):1361. doi: 10.1038/s41467-023-37037-3. PMID:36914666[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang M, He J, Li S, Cai Q, Zhang K, She J. Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter. Nat Commun. 2023 Mar 13;14(1):1361. PMID:36914666 doi:10.1038/s41467-023-37037-3
