6s2j: Difference between revisions

Latest revision as of 12:33, 24 January 2024

Square conformation of KtrA R16K mutant ring with bound ATP

Structural highlights

6s2j is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.67Å
Ligands:	ATP, MG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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:https://dx.doi.org/10.7554/eLife.50661

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OCA

[1] 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

[2] 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:https://dx.doi.org/10.7554/eLife.50661

[1]

[2]

@@ Line 3: / Line 3: @@
 <StructureSection load='6s2j' size='340' side='right'caption='[[6s2j]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6s2j]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S2J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S2J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6s2j]] is a 2 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=6S2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S2J 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.67&#8491;</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=6s2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s2j OCA], [http://pdbe.org/6s2j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s2j RCSB], [http://www.ebi.ac.uk/pdbsum/6s2j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s2j ProSAT]</span></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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6s2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s2j OCA], [https://pdbe.org/6s2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s2j RCSB], [https://www.ebi.ac.uk/pdbsum/6s2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s2j ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
 [[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: Magnesium]]
-[[Category: Potassium homeostasis]]
-[[Category: Rck domain]]
-[[Category: Square conformation octameric ring]]
-[[Category: Transport protein]]

6s2j: Difference between revisions

Latest revision as of 12:33, 24 January 2024

Square conformation of KtrA R16K mutant ring with bound ATP

Structural highlights

Function

Publication Abstract from PubMed

References

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