1lsu

<StructureSection load='1lsu' size='340' side='right' caption='[[1lsu]], [[Resolution|resolution]] 2.85&Aring;' scene=''>

<table><tr><td colspan='2'>[[1lsu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LSU FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lss|1lss]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KtrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=1lsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsu OCA], [http://pdbe.org/1lsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lsu RCSB], [http://www.ebi.ac.uk/pdbsum/1lsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsu ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/KTRA_BACSU KTRA_BACSU]] Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.<ref>PMID:12562800</ref>

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== Publication Abstract from PubMed ==

The regulation of cation content is critical for cell growth. However, the molecular mechanisms that gate the systems that control K+ movements remain unclear. KTN is a highly conserved cytoplasmic domain present ubiquitously in a variety of prokaryotic and eukaryotic K+ channels and transporters. Here we report crystal structures for two representative KTN domains that reveal a dimeric hinged assembly. Alternative ligands NAD+ and NADH block or vacate, respectively, the hinge region affecting the dimer's conformational flexibility. Conserved, surface-exposed hydrophobic patches that become coplanar upon hinge closure provide an assembly interface for KTN tetramerization. Mutational analysis using the KefC system demonstrates that this domain directly interacts with its respective transmembrane constituent, coupling ligand-mediated KTN conformational changes to the permease's activity.

A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch.,Roosild TP, Miller S, Booth IR, Choe S Cell. 2002 Jun 14;109(6):781-91. PMID:12086676<ref>PMID:12086676</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1lsu" style="background-color:#fffaf0;"></div>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Booth, I R]]

[[Category: Choe, S]]

[[Category: Miller, S]]

[[Category: Roosild, T P]]

[[Category: Ktn domain]]

[[Category: Transport protein]]