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-Structure paper
タイトル | Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 1361, Year 2023 |
掲載日 | 2023年3月13日 |
![]() | Mingxing Wang / Jin He / Shanshan Li / Qianwen Cai / Kaiming Zhang / Ji She / ![]() |
PubMed 要旨 | 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 (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. |
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手法 | EM (単粒子) |
解像度 | 3.2 - 3.5 Å |
構造データ | EMDB-34094, PDB-7ytw: EMDB-34095, PDB-7yty: |
化合物 | ![]() ChemComp-NA: ![]() ChemComp-ASC: ![]() ChemComp-HOH: |
由来 |
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![]() | STRUCTURAL PROTEIN / transporter / membrane protein / Vitamin C / sodium |