6S5E

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

6S5E の概要

• エントリーDOI: 10.2210/pdb6s5e/pdb
• 関連するPDBエントリー: 6S2J 6S5B 6S5C 6S5D
• 分子名称: Ktr system potassium uptake protein A, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: rck domain, potassium homeostasis, cation channel, non-square conformation octameric ring, atp, transport protein
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 203599.82

構造登録者

Teixeira-Duarte, C.M.,Fonseca, F.,Morais-Cabral, J.H. (登録日: 2019-07-01, 公開日: 2020-01-08, 最終更新日: 2024-01-24)

主引用文献

Teixeira-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

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

実験手法

X-RAY DIFFRACTION (3.893 Å)