7YTW

Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter

Summary for 7YTW

• Entry DOI: 10.2210/pdb7ytw/pdb
• EMDB information: 34094
• Descriptor: Solute carrier family 23 member 1, SODIUM ION, ASCORBIC ACID, ... (4 entities in total)
• Functional Keywords: transporter, membrane protein, vitamin c, sodium, structural protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 131645.08

Authors

She, J.,Wang, M.,He, J.,Zhang, K.,Li, S. (deposition date: 2022-08-16, release date: 2023-05-03, Last modification date: 2024-11-13)

Primary citation

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, 14:1361-1361, 2023

PubMed Abstract: 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.

PubMed: 36914666
DOI: 10.1038/s41467-023-37037-3

Experimental method

ELECTRON MICROSCOPY (3.2 Å)