|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6s5e' size='340' side='right'caption='[[6s5e]], [[Resolution|resolution]] 3.89Å' scene=''> | | <StructureSection load='6s5e' size='340' side='right'caption='[[6s5e]], [[Resolution|resolution]] 3.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6s5e]] is a 8 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S5E FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6s2j|6s2j]], [[6s5b|6s5b]], [[6s5c|6s5c]], [[6s5d|6s5d]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6s5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s5e OCA], [http://pdbe.org/6s5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s5e RCSB], [http://www.ebi.ac.uk/pdbsum/6s5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s5e ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fonseca, F]] | + | [[Category: Fonseca F]] |
| - | [[Category: Morais-Cabral, J H]] | + | [[Category: Morais-Cabral JH]] |
| - | [[Category: Teixeira-Duarte, C M]] | + | [[Category: Teixeira-Duarte CM]] |
| - | [[Category: Atp]]
| + | |
| - | [[Category: Cation channel]]
| + | |
| - | [[Category: Non-square conformation octameric ring]]
| + | |
| - | [[Category: Potassium homeostasis]]
| + | |
| - | [[Category: Rck domain]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holtmann G, Bakker EP, Uozumi N, Bremer E. KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity. J Bacteriol. 2003 Feb;185(4):1289-98. PMID:12562800
- ↑ Teixeira-Duarte CM, Fonseca F, Morais Cabral JH. Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site. Elife. 2019 Dec 23;8. pii: 50661. doi: 10.7554/eLife.50661. PMID:31868587 doi:http://dx.doi.org/10.7554/eLife.50661
|
