5ule: Difference between revisions

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'''Unreleased structure'''


The entry 5ule is ON HOLD
==Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant==
<StructureSection load='5ule' size='340' side='right' caption='[[5ule]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ule]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ULE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ULE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ul7|5ul7]], [[5ul9|5ul9]], [[5uld|5uld]]</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=5ule FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ule OCA], [http://pdbe.org/5ule PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ule RCSB], [http://www.ebi.ac.uk/pdbsum/5ule PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ule 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.


Authors:  
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>


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 5ule" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lu, M]]
[[Category: Transport protein]]
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