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6S5B

Non-square conformation of KtrA R16K mutant ring with bound ADP

Summary for 6S5B
Entry DOI10.2210/pdb6s5b/pdb
Related6S2J
DescriptorKtr system potassium uptake protein A, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
Functional Keywordsrck domain, potassium homeostasis, cation channel, non-square conformation octameric ring, adp, transport protein
Biological sourceBacillus subtilis subsp. subtilis str. 168
Total number of polymer chains8
Total formula weight202527.58
Authors
Teixeira-Duarte, C.M.,Fonseca, F.,Morais-Cabral, J.H. (deposition date: 2019-07-01, release date: 2020-01-08, Last modification date: 2024-01-24)
Primary citationTeixeira-Duarte, C.M.,Fonseca, F.,Morais Cabral, J.H.
Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.
Elife, 8:-, 2019
Cited by
PubMed Abstract: 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 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 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 γ-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.
PubMed: 31868587
DOI: 10.7554/eLife.50661
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.052 Å)
Structure validation

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