A channel profile report of the unusual K⁺ channel KtrB.

ABSTRACT: KtrAB is a key player in bacterial K⁺ uptake required for K⁺ homeostasis and osmoadaptation. The system is unique in structure and function. It consists of the K⁺-translocating channel subunit KtrB, which forms a dimer in the membrane, and the soluble regulatory subunit KtrA, which attaches to the cytoplasmic side of the dimer as an octameric ring conferring Na⁺ and ATP dependency to the system. Unlike most K⁺ channels, KtrB lacks the highly conserved T(X)GYG selectivity filter sequence. Instead, only a single glycine residue is found in each pore loop, which raises the question of how selective the ion channel is. Here, we characterized the KtrB subunit from the Gram-negative pathogen Vibrio alginolyticus by isothermal titratio

SUBMITTER: Mikusevic V 

PROVIDER: S-EPMC6888753 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature