Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.

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 Ca²⁺ 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 γ-phosphates of bound-ATP, tethering the two subunits and stabilizing the active st

SUBMITTER: Teixeira-Duarte CM 

PROVIDER: S-EPMC6957272 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature