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6s3k
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==KimA from Bacillus subtilis in inward-facing, occluded state== | |
| + | <StructureSection load='6s3k' size='340' side='right'caption='[[6s3k]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6s3k]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S3K FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6s3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s3k OCA], [http://pdbe.org/6s3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s3k RCSB], [http://www.ebi.ac.uk/pdbsum/6s3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s3k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6s3k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Haenelt, I]] | ||
| + | [[Category: Sousa, J S]] | ||
| + | [[Category: Tascon, I]] | ||
| + | [[Category: Vonck, J]] | ||
| + | [[Category: Leut fold]] | ||
| + | [[Category: Potassium transporter]] | ||
| + | [[Category: Smalp]] | ||
| + | [[Category: Symporter]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 04:23, 13 February 2020
KimA from Bacillus subtilis in inward-facing, occluded state
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