30uv: Difference between revisions

Latest revision as of 19:57, 29 July 2026

Structure of NaCT in Choline Chloride

Structural highlights

30uv is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.49Å
Ligands:	NAG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

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

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.^[1] ^[2]

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^[3]

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

References

↑ Inoue K, Zhuang L, Ganapathy V. Human Na+ -coupled citrate transporter: primary structure, genomic organization, and transport function. Biochem Biophys Res Commun. 2002 Dec 6;299(3):465-71. doi:, 10.1016/s0006-291x(02)02669-4. PMID:12445824 doi:https://dx.doi.org/10.1016/s0006-291x(02)02669-4
↑ Hardies K, de Kovel CG, Weckhuysen S, Asselbergh B, Geuens T, Deconinck T, Azmi A, May P, Brilstra E, Becker F, Barisic N, Craiu D, Braun KP, Lal D, Thiele H, Schubert J, Weber Y, van 't Slot R, Nurnberg P, Balling R, Timmerman V, Lerche H, Maudsley S, Helbig I, Suls A, Koeleman BP, De Jonghe P. Recessive mutations in SLC13A5 result in a loss of citrate transport and cause neonatal epilepsy, developmental delay and teeth hypoplasia. Brain. 2015 Nov;138(Pt 11):3238-50. doi: 10.1093/brain/awv263. Epub 2015 Sep 17. PMID:26384929 doi:https://dx.doi.org/10.1093/brain/awv263
↑ Sauer DB, Song J, Marden JJ, Wang B, Sowerby K, Sudar JC, Rice WJ, Wang DN. Structures of the human sodium-citrate cotransporter NaCT with and without substrates. bioRxiv [Preprint]. 2026 Jul 12:2026.07.08.737274. doi: , 10.64898/2026.07.08.737274. PMID:42465234 doi:https://dx.doi.org/10.64898/2026.07.08.737274

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OCA

[1] Inoue K, Zhuang L, Ganapathy V. Human Na+ -coupled citrate transporter: primary structure, genomic organization, and transport function. Biochem Biophys Res Commun. 2002 Dec 6;299(3):465-71. doi:, 10.1016/s0006-291x(02)02669-4. PMID:12445824 doi:https://dx.doi.org/10.1016/s0006-291x(02)02669-4

[2] Hardies K, de Kovel CG, Weckhuysen S, Asselbergh B, Geuens T, Deconinck T, Azmi A, May P, Brilstra E, Becker F, Barisic N, Craiu D, Braun KP, Lal D, Thiele H, Schubert J, Weber Y, van 't Slot R, Nurnberg P, Balling R, Timmerman V, Lerche H, Maudsley S, Helbig I, Suls A, Koeleman BP, De Jonghe P. Recessive mutations in SLC13A5 result in a loss of citrate transport and cause neonatal epilepsy, developmental delay and teeth hypoplasia. Brain. 2015 Nov;138(Pt 11):3238-50. doi: 10.1093/brain/awv263. Epub 2015 Sep 17. PMID:26384929 doi:https://dx.doi.org/10.1093/brain/awv263

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

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 30uv is ON HOLD  until Paper Publication
+==Structure of NaCT in Choline Chloride==
+<StructureSection load='30uv' size='340' side='right'caption='[[30uv]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[30uv]] 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=30UV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30UV 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]] 2.49&#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=30uv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30uv OCA], [https://pdbe.org/30uv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30uv RCSB], [https://www.ebi.ac.uk/pdbsum/30uv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30uv 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 30uv" 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]]

30uv: Difference between revisions

Latest revision as of 19:57, 29 July 2026

Structure of NaCT in Choline Chloride

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

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