This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

6s5e

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Non-square conformation of KtrA A80P mutant ring with bound ATP

Structural highlights

6s5e is a 8 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 3.893Å
Ligands:
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:http://dx.doi.org/10.7554/eLife.50661

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6s5e"

Categories: Bacillus subtilis subsp. subtilis str. 168 | Large Structures | Fonseca F | Morais-Cabral JH | Teixeira-Duarte CM

@@ Line 3: / Line 3: @@
 <StructureSection load='6s5e' size='340' side='right'caption='[[6s5e]], [[Resolution|resolution]] 3.89&Aring;' scene=''>
 == 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]] 3.893&#8491;</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>
 == 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 23: / 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: Non-square conformation octameric ring]]
-[[Category: Potassium homeostasis]]
-[[Category: Rck domain]]
-[[Category: Transport protein]]

6s5e

From Proteopedia

Current revision

Non-square conformation of KtrA A80P mutant ring with bound ATP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox