ArticlePLoS biology2016
Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter.
Article in PLoS biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- A short intrinsically disordered region at KtrB's N-terminus facilitates allosteric regulation of KNature communications · 2025Article
- Structural basis and synergism of ATP and NaNature communications · 2024Article
- c-di-AMP determines the hierarchical organization of bacterial RCK proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural insights into ion selectivity and transport mechanisms of Oryza sativa HKT2;1 and HKT2;2/1 transporters.Nature plants · 2024Article
- N-Terminus Plays a Critical Role for Stabilizing the Filamentous Assembly and the Antifungal Activity of Bg_9562.Microbiology spectrum · 2022Article
- Molecular Mechanisms for Bacterial Potassium Homeostasis.Journal of molecular biology · 2021Review
- c-di-AMP-Regulated KInfection and immunity · 2021Article
- Fluorometric Liposome Screen for Inhibitors of a Physiologically Important Bacterial Ion Channel.Frontiers in microbiology · 2021Article
- Two Ways To Convert a Low-Affinity Potassium Channel to High Affinity: Control of Bacillus subtilis KtrCD by Glutamate.Journal of bacteriology · 2020Article
- Whole Genome Sequencing and Comparative Genomic Analyses ofMicroorganisms · 2020Article
- TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential.Nature communications · 2020Article
- Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.eLife · 2019Article
- A channel profile report of the unusual KThe Journal of general physiology · 2019Article
- Why Nature Chose Potassium.Journal of molecular evolution · 2019Review
- Compatible Solute Synthesis and Import by the Moderate HalophileFrontiers in microbiology · 2018Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.