Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter

PLoS Biology
Andras SzollosiJoão H Morais-Cabral

Abstract

KtrAB belongs to the Trk/Ktr/HKT superfamily of monovalent cation (K+ and Na+) transport proteins that closely resemble K+ channels. These proteins underlie a plethora of cellular functions that are crucial for environmental adaptation in plants, fungi, archaea, and bacteria. The activation mechanism of the Trk/Ktr/HKT proteins remains unknown. It has been shown that ATP stimulates the activity of KtrAB while ADP does not. Here, we present X-ray structural information on the KtrAB complex with bound ADP. A comparison with the KtrAB-ATP structure reveals conformational changes in the ring and in the membrane protein. In combination with a biochemical and functional analysis, we uncover how ligand-dependent changes in the KtrA ring are propagated to the KtrB membrane protein and conclude that, despite their structural similarity, the activation mechanism of KtrAB is markedly different from the activation mechanism of K+ channels.

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Citations

Oct 30, 2019·Journal of Molecular Evolution·Antoine Danchin, Pablo Iván Nikel
Oct 19, 2019·The Journal of General Physiology·Vedrana MikuševićInga Hänelt
Mar 19, 2021·Frontiers in Microbiology·Andreia S FernandesCarol A Harley
Mar 4, 2020·Biochimica Et Biophysica Acta. Biomembranes·George L OrrissJörg Stetefeld
Apr 3, 2021·Journal of Molecular Biology·Janina StautzInga Hänelt

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Datasets Mentioned

BETA
KIX81591.1
KIX81590.1

Methods Mentioned

BETA
electron paramagnetic resonance
size-exclusion chromatography
Assay

Software Mentioned

PHENIX
PHASER
DMmulti
XDS
LLG

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