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Structure and mechanism of the K+/H+ exchanger KefC
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Structure and mechanism of the K+/H+ exchanger KefC
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Journal Article
Structure and mechanism of the K+/H+ exchanger KefC
2024
Overview
Intracellular potassium (K
+
) homeostasis is fundamental to cell viability. In addition to channels, K
+
levels are maintained by various ion transporters. One major family is the proton-driven K
+
efflux transporters, which in gram-negative bacteria is important for detoxification and in plants is critical for efficient photosynthesis and growth. Despite their importance, the structure and molecular basis for K
+
-selectivity is poorly understood. Here, we report ~3.1 Å resolution cryo-EM structures of the
Escherichia coli
glutathione (GSH)-gated K
+
efflux transporter KefC in complex with AMP, AMP/GSH and an ion-binding variant. KefC forms a homodimer similar to the inward-facing conformation of Na
+
/H
+
antiporter NapA. By structural assignment of a coordinated K
+
ion, MD simulations, and SSM-based electrophysiology, we demonstrate how ion-binding in KefC is adapted for binding a dehydrated K
+
ion. KefC harbors C-terminal regulator of K
+
conductance (RCK) domains, as present in some bacterial K
+
-ion channels. The domain-swapped helices in the RCK domains bind AMP and GSH and they inhibit transport by directly interacting with the ion-transporter module. Taken together, we propose that KefC is activated by detachment of the RCK domains and that ion selectivity exploits the biophysical properties likewise adapted by K
+
-ion-channels.
Intracellular potassium (K+) homeostasis is achieved by activity of both ion channels and transporters. Here, the authors report structures of
E. coli
glutathione (GSH)-gated K+ efflux transporter KefC with bound K+ and conclude that the ion-binding site is adapted for binding a dehydrated ion.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/16
/ 82/80
/ 82/83
/ 9/10
/ AMP
/ Bacteria
/ biokemi
/ E coli
/ Efflux
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Helices
/ Humanities and Social Sciences
/ Molecular Dynamics Simulation
/ Potassium-Hydrogen Antiporters - chemistry
/ Potassium-Hydrogen Antiporters - genetics
/ Potassium-Hydrogen Antiporters - metabolism
/ Science
