Evidence map›Paper›PMID 23598340›Full record

ArticleNature2013

The structure of the KtrAB potassium transporter.

Ricardo S Vieira-Pires, Andras Szollosi, João H Morais-Cabral

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
15.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 113 citations in OpenAlex.

  1. Ionic-Bionic Interfaces: Advancing Iontronic Strategies for Bioelectronic Sensing and Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. c-di-AMP determines the hierarchical organization of bacterial RCK proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Inverse regulation of SOS1 and HKT1 protein localization and stability by SOS3/CBL4 inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Membrane Targeted Azobenzene Drives Optical Modulation of Bacterial Membrane Potential.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  9. Dimerisation of the Yeast KInternational journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. Assembly and Analysis of Cell-Scale Membrane Envelopes.Journal of chemical information and modeling · 2022
    Article
  13. Review
  14. Unappreciated Roles for KTrends in microbiology · 2021
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. c-di-AMP-Regulated KInfection and immunity · 2021
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ricardo S Vieira-PiresInstituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal.
Andras Szollosi
João H Morais-Cabral
Universidade do Porto · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacteria, archaea, fungi and plants the Trk, Ktr and HKT ion transporters are key components of osmotic regulation, pH homeostasis and resistance to drought and high salinity. These ion transporters are functionally diverse: they can function as Na(+) or K(+) channels and possibly as cation/K(+) symporters. They are closely related to potassium channels both at the level of the membrane protein and at the level of the cytosolic regulatory domains. Here we describe the crystal structure of a Ktr K(+) transporter, the KtrAB complex from Bacillus subtilis. The structure shows the dimeric membrane protein KtrB assembled with a cytosolic octameric KtrA ring bound to ATP, an activating ligand. A comparison between the structure of KtrAB-ATP and the structures of the isolated full-length KtrA protein with ATP or ADP reveals a ligand-dependent conformational change in the octameric ring, raising new ideas about the mechanism of activation in these transporters.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBacillus subtilisBacterial ProteinsCation Transport ProteinsCrystallography, X-RayIon TransportModels, BiologicalModels, MolecularPotassiumProtein ConformationProtein SubunitsStructure-Activity RelationshipAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsCation Transport ProteinsKtrB protein, BacteriaPotassiumProtein Subunits

Identifiers

PMID23598340
OpenAlexW2135737750

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.