KTN (RCK) domains regulate K+ channels and transporters by controlling the dimer-hinge conformation.

ABSTRACT: KTN (RCK) domains are nucleotide-binding folds that form the cytoplasmic regulatory complexes of various K+ channels and transporters. The mechanisms these proteins use to control their transmembrane pore-forming counterparts remains unclear despite numerous electrophysiological and structural studies. KTN (RCK) domains consistently crystallize as dimers within the asymmetric unit, forming a pronounced hinge between two Rossmann folds. We have previously proposed that modification of the hinge angle plays an important role in activating the associated membrane-integrated components of the channel or transporter. Here we report the structure of the C-terminal, KTN-bearing domain of the E. coli KefC K+ efflux system in association with the ancillary subunit, KefF, which is known to stabilize

SUBMITTER: Roosild TP 

PROVIDER: S-EPMC2920069 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature