30uu: Difference between revisions

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'''Unreleased structure'''


The entry 30uu is ON HOLD  until Paper Publication
==Structure of NaCT in NaCl==
<StructureSection load='30uu' size='340' side='right'caption='[[30uu]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[30uu]] 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=30UU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30UU 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]] 2.51&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=30uu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30uu OCA], [https://pdbe.org/30uu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30uu RCSB], [https://www.ebi.ac.uk/pdbsum/30uu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30uu 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 30uu" 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]]
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