View source for 6wtw


==Structure of LaINDY crystallized in the presence of alpha-ketoglutarate and malate==
<StructureSection load='6wtw' size='340' side='right'caption='[[6wtw]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wtw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_acidophilus Lactobacillus acidophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WTW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.86&#8491;</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=6wtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wtw OCA], [https://pdbe.org/6wtw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wtw RCSB], [https://www.ebi.ac.uk/pdbsum/6wtw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wtw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5FKK5_LACAC Q5FKK5_LACAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Citrate, alpha-ketoglutarate and succinate are TCA cycle intermediates that also play essential roles in metabolic signaling and cellular regulation. These di- and tricarboxylates are imported into the cell by the divalent anion sodium symporter (DASS) family of plasma membrane transporters, which contains both cotransporters and exchangers. While DASS proteins transport substrates via an elevator mechanism, to date structures are only available for a single DASS cotransporter protein in a substrate-bound, inward-facing state. We report multiple cryo-EM and X-ray structures in four different states, including three hitherto unseen states, along with molecular dynamics simulations, of both a cotransporter and an exchanger. Comparison of these outward- and inward-facing structures reveal how the transport domain translates and rotates within the framework of the scaffold domain through the transport cycle. Additionally, we propose that DASS transporters ensure substrate coupling by a charge-compensation mechanism, and by structural changes upon substrate release.

Structural basis for the reaction cycle of DASS dicarboxylate transporters.,Sauer DB, Trebesch N, Marden JJ, Cocco N, Song J, Koide A, Koide S, Tajkhorshid E, Wang DN Elife. 2020 Sep 1;9. pii: 61350. doi: 10.7554/eLife.61350. PMID:32869741<ref>PMID:32869741</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wtw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactobacillus acidophilus]]
[[Category: Large Structures]]
[[Category: Cocco N]]
[[Category: Marden JJ]]
[[Category: Sauer DB]]
[[Category: Song JM]]
[[Category: Wang DN]]