5ul7: Difference between revisions
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==Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant== | ==Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant== | ||
<StructureSection load='5ul7' size='340' side='right' caption='[[5ul7]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5ul7' size='340' side='right'caption='[[5ul7]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ul7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL7 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5ul7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UL7 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> | </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=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ul9|5ul9]], [[5uld|5uld]], [[5ule|5ule]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ul9|5ul9]], [[5uld|5uld]], [[5ule|5ule]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC_A0025 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ul7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul7 OCA], [http://pdbe.org/5ul7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ul7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ul7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ul7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ul7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Symporter 3D structures|Symporter 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Vibch]] | |||
[[Category: Lu, M]] | [[Category: Lu, M]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 15:38, 23 September 2020
Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variantStructure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant
Structural highlights
Publication Abstract from PubMedIntegral 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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