ArticleStructure (London, England : 1993)2009
KTN (RCK) domains regulate K+ channels and transporters by controlling the dimer-hinge conformation.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed.
- Modular architecture of KEMBO reports · 2025Review
- Structure and mechanism of the KNature communications · 2024Article
- The Potassium Efflux System Kef: Bacterial Protection against Toxic Electrophilic Compounds.Membranes · 2023Review
- The allosteric gating mechanism of the MthK channel.National science review · 2022Article
- Impaired photoprotection in Phaeodactylum tricornutum KEA3 mutants reveals the proton regulatory circuit of diatoms light acclimation.The New phytologist · 2022Article
- Impact of ion fluxes across thylakoid membranes on photosynthetic electron transport and photoprotection.Nature plants · 2021Article
- Stromal NADH supplied by PHOSPHOGLYCERATE DEHYDROGENASE3 is crucial for photosynthetic performance.Plant physiology · 2021Article
- Silencing ofFrontiers in plant science · 2021Article
- The topology of plastid inner envelope potassium cation efflux antiporter KEA1 provides new insights into its regulatory features.Photosynthesis research · 2020Article
- Diverse Physiological Functions of Cation Proton Antiporters across Bacteria and Plant Cells.International journal of molecular sciences · 2020Review
- Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.eLife · 2019Article
- Evidence for potassium transport activity of Arabidopsis KEA1-KEA6.Scientific reports · 2019Article
- Annotation of the Giardia proteome through structure-based homology and machine learning.GigaScience · 2019Article
- Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System.Biochemistry · 2017Article
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- Transcriptomics Indicates Active and Passive Metronidazole Resistance Mechanisms in Three SeminalFrontiers in microbiology · 2017Article
- Regulation and Levels of the Thylakoid K+/H+ Antiporter KEA3 Shape the Dynamic Response of Photosynthesis in Fluctuating Light.Plant & cell physiology · 2016Article
- Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015Review
- Understanding the structural requirements for activators of the Kef bacterial potassium efflux system.Biochemistry · 2014Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
KTN (RCK) domains are nucleotide-binding folds that form the cytoplasmic regulatory complexes of various K+ channels and transporters. The mechanisms these proteins use to control their transmembrane pore-forming counterparts remains unclear despite numerous electrophysiological and structural studies. KTN (RCK) domains consistently crystallize as dimers within the asymmetric unit, forming a pronounced hinge between two Rossmann folds. We have previously proposed that modification of the hinge angle plays an important role in activating the associated membrane-integrated components of the channel or transporter. Here we report the structure of the C-terminal, KTN-bearing domain of the E. coli KefC K+ efflux system in association with the ancillary subunit, KefF, which is known to stabilize the conductive state. The structure of the complex and functional analysis of KefC variants reveal that control of the conformational flexibility inherent in the KTN dimer hinge is modulated by KefF and essential for regulation of KefC ion flux.
Indexed as
Identifiers
What OpenQuestion holds
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.