7ytw

From Proteopedia

(Difference between revisions)

Current revision

Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter

Structural highlights

7ytw is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Toyoda Y, Miyata H, Uchida N, Morimoto K, Shigesawa R, Kassai H, Nakao K, Tomioka NH, Matsuo H, Ichida K, Hosoyamada M, Aiba A, Suzuki H, Takada T. Vitamin C transporter SVCT1 serves a physiological role as a urate importer: functional analyses and in vivo investigations. Pflugers Arch. 2023 Apr;475(4):489-504. PMID:36749388 doi:10.1007/s00424-023-02792-1
↑ Wang M, He J, Li S, Cai Q, Zhang K, She J. Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter. Nat Commun. 2023 Mar 13;14(1):1361. PMID:36914666 doi:10.1038/s41467-023-37037-3

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7ytw"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7ytw]] 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=7YTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YTW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=7ytw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ytw OCA], [https://pdbe.org/7ytw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ytw RCSB], [https://www.ebi.ac.uk/pdbsum/7ytw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ytw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/S23A1_MOUSE S23A1_MOUSE] Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.[UniProtKB:Q9UHI7]
+[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 ==

7ytw

From Proteopedia

Current revision

Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter

Structural highlights

Function

Publication Abstract from PubMed

References

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