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TitleDimeric transport mechanism of human vitamin C transporter SVCT1.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5569, Year 2024
Publish dateJul 2, 2024
AuthorsTakaaki A Kobayashi / Hiroto Shimada / Fumiya K Sano / Yuzuru Itoh / Sawako Enoki / Yasushi Okada / Tsukasa Kusakizako / Osamu Nureki /
PubMed AbstractVitamin 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 ...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.
External linksNat Commun / PubMed:38956111 / PubMed Central
MethodsEM (single particle)
Resolution2.49 - 3.5 Å
Structure data

36201

8jew

EMDB-36201, PDB-8jew:
Human sodium-dependent vitamin C transporter 1 bound to L-ascorbic acid in an inward-open state
Method: EM (single particle) / Resolution: 2.49 Å

36204

8jez

EMDB-36204, PDB-8jez:
Human sodium-dependent vitamin C transporter 1 in an apo inward-open state
Method: EM (single particle) / Resolution: 2.6 Å

36205

8jf0

EMDB-36205, PDB-8jf0:
Human sodium-dependent vitamin C transporter 1 in an intermediate state
Method: EM (single particle) / Resolution: 3.5 Å

36206

8jf1

EMDB-36206, PDB-8jf1:
Human sodium-dependent vitamin C transporter 1 in an apo occluded state
Method: EM (single particle) / Resolution: 2.85 Å

Chemicals

ChemComp-ASC:
ASCORBIC ACID / medication*YM

ChemComp-NA:
Unknown entry

ChemComp-AV0:
Lauryl Maltose Neopentyl Glycol

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM

ChemComp-CLR:
CHOLESTEROL

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PLM:
PALMITIC ACID

ChemComp-HOH:
WATER

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Transporter / Membrane protein / Ascorbic acid / Vitamin C / Sodium / Solute carrier

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