8jf0: Difference between revisions
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New page: '''Unreleased structure''' The entry 8jf0 is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Human sodium-dependent vitamin C transporter 1 in an intermediate state== | |||
<StructureSection load='8jf0' size='340' side='right'caption='[[8jf0]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8jf0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JF0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8jf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jf0 OCA], [https://pdbe.org/8jf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jf0 RCSB], [https://www.ebi.ac.uk/pdbsum/8jf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jf0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/S23A1_HUMAN S23A1_HUMAN] Sodium:ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate (PubMed:10556483, PubMed:10556521, PubMed:10631088, PubMed:36749388). Has retained some ancestral activity toward nucleobases such as urate, an oxidized purine. Low-affinity high-capacity sodium:urate cotransporter, may regulate serum urate levels by serving as a renal urate re-absorber (PubMed:36749388).<ref>PMID:10556483</ref> <ref>PMID:10556521</ref> <ref>PMID:10631088</ref> <ref>PMID:36749388</ref> Inactive transporter.<ref>PMID:10556483</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A 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. | |||
Dimeric transport mechanism of human vitamin C transporter SVCT1.,Kobayashi TA, Shimada H, Sano FK, Itoh Y, Enoki S, Okada Y, Kusakizako T, Nureki O Nat Commun. 2024 Jul 2;15(1):5569. doi: 10.1038/s41467-024-49899-2. PMID:38956111<ref>PMID:38956111</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8jf0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Kobayashi TA]] | |||
[[Category: Kusakizako T]] | |||
[[Category: Nureki O]] | |||
