View source for 7yty


==Mouse SVCT1 in an apo state==
<StructureSection load='7yty' size='340' side='right'caption='[[7yty]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yty]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YTY 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]] 3.5&#8491;</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=7yty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yty OCA], [https://pdbe.org/7yty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yty RCSB], [https://www.ebi.ac.uk/pdbsum/7yty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yty ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S23A1_MOUSE S23A1_MOUSE] Sodium:L-ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each L-ascorbate (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 (By similarity) (PubMed:36749388).[UniProtKB:Q9UHI7]<ref>PMID:36749388</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter.,Wang M, He J, Li S, Cai Q, Zhang K, She J Nat Commun. 2023 Mar 13;14(1):1361. doi: 10.1038/s41467-023-37037-3. PMID:36914666<ref>PMID:36914666</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yty" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: He J]]
[[Category: Li S]]
[[Category: She J]]
[[Category: Wang M]]
[[Category: Zhang K]]