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5ul9
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant== | |
| + | <StructureSection load='5ul9' size='340' side='right' caption='[[5ul9]], [[Resolution|resolution]] 2.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ul9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UL9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ul7|5ul7]], [[5uld|5uld]], [[5ule|5ule]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ul9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul9 OCA], [http://pdbe.org/5ul9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ul9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ul9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Integral membrane proteins of the divalent anion/Na+ symporter (DASS) family translocate dicarboxylate, tricarboxylate or sulphate across cell membranes, typically by utilizing the preexisting Na+ gradient. The molecular determinants for substrate recognition by DASS remain obscure, largely owing to the absence of any substrate-bound DASS structure. Here we present 2.8-A resolution X-ray structures of VcINDY, a DASS from Vibrio cholerae that catalyses the co-transport of Na+ and succinate. These structures portray the Na+-bound VcINDY in complexes with succinate and citrate, elucidating the binding sites for substrate and two Na+ ions. Furthermore, we report the structures of a humanized variant of VcINDY in complexes with succinate and citrate, which predict how a human citrate-transporting DASS may interact with its bound substrate. Our findings provide insights into metabolite transport by DASS, establishing a molecular basis for future studies on the regulation of this transport process. | ||
| - | + | Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant.,Nie R, Stark S, Symersky J, Kaplan RS, Lu M Nat Commun. 2017 Apr 24;8:15009. doi: 10.1038/ncomms15009. PMID:28436435<ref>PMID:28436435</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ul9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lu, M]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 15:40, 17 May 2017
Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant
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