Lipid-protein interactions modulate the conformational equilibrium of a potassium channel.

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ID: 106049
2020
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Abstract
Cell membranes actively participate in the regulation of protein structure and function. In this work, we conduct molecular dynamics simulations to investigate how different membrane environments affect protein structure and function in the case of MthK, a potassium channel. We observe different ion permeation rates of MthK in membranes with different properties, and ascribe them to a shift of the conformational equilibrium between two states of the channel that differ according to whether a transmembrane helix has a kink. Further investigations indicate that two key residues in the kink region mediate a crosstalk between two gates at the selectivity filter and the central cavity, respectively. Opening of one gate eventually leads to closure of the other. Our simulations provide an atomistic model of how lipid-protein interactions affect the conformational equilibrium of a membrane protein. The gating mechanism revealed for MthK may also apply to other potassium channels.
Reference Key
gu2020lipidproteinnature Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Gu, Ruo-Xu;de Groot, Bert L;
Journal Nature communications
Year 2020
DOI
10.1038/s41467-020-15741-8
URL
Keywords
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