6s5e
From Proteopedia
(Difference between revisions)
m (Protected "6s5e" [edit=sysop:move=sysop]) |
|||
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Non-square conformation of KtrA A80P mutant ring with bound ATP== | |
| + | <StructureSection load='6s5e' size='340' side='right'caption='[[6s5e]], [[Resolution|resolution]] 3.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6s5e]] is a 8 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=6S5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S5E 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]] 3.893Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=6s5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s5e OCA], [https://pdbe.org/6s5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s5e RCSB], [https://www.ebi.ac.uk/pdbsum/6s5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s5e 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6s5e" 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]] | ||
Current revision
Non-square conformation of KtrA A80P mutant ring with bound ATP
| |||||||||||
