Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.

ABSTRACT: The conformational changes required for activation and K⁺ conduction in inward-rectifier K⁺ (Kir) channels are still debated. These structural changes are brought about by lipid binding. It is unclear how this process relates to fast gating or if the intracellular and extracellular regions of the protein are coupled. Here, we examine the structural details of KirBac1.1 reconstituted into both POPC and an activating lipid mixture of 3:2 POPC:POPG (wt/wt). KirBac1.1 is a prokaryotic Kir channel that shares homology with human Kir channels. We establish that KirBac1.1 is in a constitutively active state in POPC:POPG bilayers through the use of real-time fluorescence quenching assays and Förster resonance energy transfer (FRET) distance measurements. Multidimensional soli

SUBMITTER: Amani R 

PROVIDER: S-EPMC7022178 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature