View source for 6s7r


==Non-square conformations of KtrA R16A mutant rings with bound ADP==
<StructureSection load='6s7r' size='340' side='right'caption='[[6s7r]], [[Resolution|resolution]] 3.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6s7r]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S7R 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]] 3.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=6s7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s7r OCA], [https://pdbe.org/6s7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s7r RCSB], [https://www.ebi.ac.uk/pdbsum/6s7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s7r ProSAT]</span></td></tr>
</table>
== Function ==
[https://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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RCK domains regulate the activity of K(+) channels and transporters in eukaryotic and prokaryotic organisms by responding to ions or nucleotides. The mechanisms of RCK activation by Ca(2+) in the eukaryotic BK and bacterial MthK K(+) channels are well understood. However, the molecular details of activation in nucleotide-dependent RCK domains are not clear. Through a functional and structural analysis of the mechanism of ATP activation in KtrA, a RCK domain from the B. subtilis KtrAB cation channel, we have found that activation by nucleotide requires binding of cations to an intra-dimer interface site in the RCK dimer. In particular, divalent cations are coordinated by the gamma-phosphates of bound-ATP, tethering the two subunits and stabilizing the active state conformation. Strikingly, the binding site residues are highly conserved in many different nucleotide-dependent RCK domains, indicating that divalent cations are a general cofactor in the regulatory mechanism of many nucleotide-dependent RCK domains.

Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.,Teixeira-Duarte CM, Fonseca F, Morais Cabral JH Elife. 2019 Dec 23;8. pii: 50661. doi: 10.7554/eLife.50661. PMID:31868587<ref>PMID:31868587</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6s7r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Fonseca F]]
[[Category: Morais-Cabral JH]]
[[Category: Teixeira-Duarte CM]]