Dimeric transport mechanism of human vitamin C transporter SVCT1

Takaaki A. Kobayashi, Hiroto Shimada, Fumiya K. Sano, Yuzuru Itoh, Sawako Enoki, Yasushi Okada, Tsukasa Kusakizako () and Osamu Nureki ()
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Takaaki A. Kobayashi: The University of Tokyo
Hiroto Shimada: The University of Tokyo
Fumiya K. Sano: The University of Tokyo
Yuzuru Itoh: The University of Tokyo
Sawako Enoki: The University of Tokyo
Yasushi Okada: The University of Tokyo
Tsukasa Kusakizako: The University of Tokyo
Osamu Nureki: The University of Tokyo

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Vitamin C plays important roles as a cofactor in many enzymatic reactions and as an antioxidant against oxidative stress. As some mammals including humans cannot synthesize vitamin C de novo from glucose, its uptake from dietary sources is essential, and is mediated by the sodium-dependent vitamin C transporter 1 (SVCT1). Despite its physiological significance in maintaining vitamin C homeostasis, the structural basis of the substrate transport mechanism remained unclear. Here, we report the cryo-EM structures of human SVCT1 in different states at 2.5–3.5 Å resolutions. The binding manner of vitamin C together with two sodium ions reveals the counter ion-dependent substrate recognition mechanism. Furthermore, comparisons of the inward-open and occluded structures support a transport mechanism combining elevator and distinct rotational motions. Our results demonstrate the molecular mechanism of vitamin C transport with its underlying conformational cycle, potentially leading to future industrial and medical applications.

Date: 2024
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DOI: 10.1038/s41467-024-49899-2

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