View source for 30ut


==Structure of the NaCT-Na-PF2 complex==
<StructureSection load='30ut' size='340' side='right'caption='[[30ut]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[30ut]] is a 2 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=30UT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30UT 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]] 2.53&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=X3M:(2R)-2-[2-(4-tert-butylphenyl)ethyl]-2-hydroxybutanedioic+acid'>X3M</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=30ut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30ut OCA], [https://pdbe.org/30ut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30ut RCSB], [https://www.ebi.ac.uk/pdbsum/30ut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30ut ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/S13A5_HUMAN S13A5_HUMAN] Undetermined early-onset epileptic encephalopathy;Amelocerebrohypohidrotic syndrome;Pyridoxine-dependent epilepsy. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/S13A5_HUMAN S13A5_HUMAN] High-affinity sodium/citrate cotransporter that mediates citrate entry into cells. The transport process is electrogenic; it is the trivalent form of citrate rather than the divalent form that is recognized as a substrate. May facilitate the utilization of circulating citrate for the generation of metabolic energy and for the synthesis of fatty acids and cholesterol.<ref>PMID:12445824</ref> <ref>PMID:26384929</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human sodium-citrate cotransporter NaCT imports various tri- and dicarboxylates into the cell as TCA cycle intermediates. This substrate uptake process is driven by an inward sodium gradient. The protein is a member of the Divalent Anion-Sodium Symporter (DASS) family. Whereas extensive biochemical and structural studies have been carried out for NaCT, how the substrate binding and translocation is coupled to the sodium gradient remains unclear. Here using single particle cryo-electron microscopy, we determined the structures of the human NaCT protein in three states: sodium-free, in the presence of sodium, and sodium- and substrate-bound. These structures suggest a simultaneous binding mechanism for sodium-substrate coupling, distinct from the sequential binding, conformational selection mechanism previously observed for the bacterial DASS protein VcINDY.

Structures of the human sodium-citrate cotransporter NaCT with and without substrates.,Sauer DB, Song J, Marden JJ, Wang B, Sowerby K, Sudar JC, Rice WJ, Wang DN bioRxiv [Preprint]. 2026 Jul 12:2026.07.08.737274. doi: , 10.64898/2026.07.08.737274. PMID:42465234<ref>PMID:42465234</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 30ut" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Marden JJ]]
[[Category: Rice WJ]]
[[Category: Sauer DB]]
[[Category: Song J]]
[[Category: Wang B]]
[[Category: Wang DN]]