6s3k: Difference between revisions

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New page: '''Unreleased structure''' The entry 6s3k is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6s3k is ON HOLD
==KimA from Bacillus subtilis in inward-facing, occluded state==
<SX load='6s3k' size='340' side='right' viewer='molstar' caption='[[6s3k]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6s3k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S3K 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]] 3.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=6s3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s3k OCA], [https://pdbe.org/6s3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s3k RCSB], [https://www.ebi.ac.uk/pdbsum/6s3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s3k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KIMA_BACSU KIMA_BACSU] High-affinity potassium transporter (PubMed:28420751, PubMed:32005818). Functions as a K(+)/H(+) symporter (PubMed:32005818).<ref>PMID:28420751</ref> <ref>PMID:32005818</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Potassium homeostasis is vital for all organisms, but is challenging in single-celled organisms like bacteria and yeast and immobile organisms like plants that constantly need to adapt to changing external conditions. KUP transporters facilitate potassium uptake by the co-transport of protons. Here, we uncover the molecular basis for transport in this widely distributed family. We identify the potassium importer KimA from Bacillus subtilis as a member of the KUP family, demonstrate that it functions as a K(+)/H(+) symporter and report a 3.7 A cryo-EM structure of the KimA homodimer in an inward-occluded, trans-inhibited conformation. By introducing point mutations, we identify key residues for potassium and proton binding, which are conserved among other KUP proteins.


Authors:  
Structural basis of proton-coupled potassium transport in the KUP family.,Tascon I, Sousa JS, Corey RA, Mills DJ, Griwatz D, Aumuller N, Mikusevic V, Stansfeld PJ, Vonck J, Hanelt I Nat Commun. 2020 Jan 31;11(1):626. doi: 10.1038/s41467-020-14441-7. PMID:32005818<ref>PMID:32005818</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 6s3k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Haenelt I]]
[[Category: Sousa JS]]
[[Category: Tascon I]]
[[Category: Vonck J]]
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