ArticleNature2017
Crystal structure of the potassium-importing KdpFABC membrane complex.
Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 82 citations in OpenAlex.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Lipids are essential for potassium transport by KdpFABC from E. coli.bioRxiv : the preprint server for biology · 2026Article
- On the mechanism of K+ transport through the inter-subunit tunnel of KdpFABC.The Journal of general physiology · 2026Article
- Three plant growth-promoting rhizobacteria from the Qinghai-Tibet Plateau enhanced plant growth and alleviated low-temperature and drought stress.Frontiers in plant science · 2026Article
- Conduction pathway for potassium through theeLife · 2025Article
- Conduction pathway for potassium through the E. coli pump KdpFABC.bioRxiv : the preprint server for biology · 2025Article
- P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025Article
- High-throughput discovery of inhibitory protein fragments with AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- High-throughput discovery of inhibitory protein fragments with AlphaFold.bioRxiv : the preprint server for biology · 2024Article
- Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024Review
- KdpD is a tandem serine histidine kinase that controls KNature communications · 2024Article
- Enhancing coevolutionary signals in protein-protein interaction prediction through clade-wise alignment integration.Scientific reports · 2024Article
- The First Quarter Century of the Dense Alignment Surface Transmembrane Prediction Method.International journal of molecular sciences · 2023Article
- The Potassium Efflux System Kef: Bacterial Protection against Toxic Electrophilic Compounds.Membranes · 2023Review
- Review
- Dimerisation of the Yeast KInternational journal of molecular sciences · 2022Article
- Article
- Mapping functional regions of essential bacterial proteins with dominant-negative protein fragments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Cellular potassium import systems play a fundamental role in osmoregulation, pH homeostasis and membrane potential in all domains of life. In bacteria, the kdp operon encodes a four-subunit potassium pump that maintains intracellular homeostasis, cell shape and turgor under conditions in which potassium is limiting. This membrane complex, called KdpFABC, has one channel-like subunit (KdpA) belonging to the superfamily of potassium transporters and another pump-like subunit (KdpB) belonging to the superfamily of P-type ATPases. Although there is considerable structural and functional information about members of both superfamilies, the mechanism by which uphill potassium transport through KdpA is coupled with ATP hydrolysis by KdpB remains poorly understood. Here we report the 2.9 Å X-ray structure of the complete Escherichia coli KdpFABC complex with a potassium ion within the selectivity filter of KdpA and a water molecule at a canonical cation site in the transmembrane domain of KdpB. The structure also reveals two structural elements that appear to mediate the coupling between these two subunits. Specifically, a protein-embedded tunnel runs between these potassium and water sites and a helix controlling the cytoplasmic gate of KdpA is linked to the phosphorylation domain of KdpB. On the basis of these observations, we propose a mechanism that repurposes protein channel architecture for active transport across biomembranes.
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.