Evidence map›Paper›PMID 22231399›Full record

ArticleNature structural & molecular biology2012

Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating.

Vassiliy N Bavro, Rita De Zorzi, Matthias R Schmidt, João R C Muniz, Lejla Zubcevic, Mark S P Sansom, Catherine Vénien-Bryan, Stephen J Tucker

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

68 citing papers in PubMed, 94 citations in OpenAlex.

  1. Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026
    Review
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  13. Vascular KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Simulating PIPFrontiers in molecular biosciences · 2021
    Article
  16. Asymmetric Interplay Between KFrontiers in physiology · 2021
    Article
  17. Article
  18. The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020
    Article
  19. Article
  20. Article

8 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 3 countries.

Vassiliy N BavroClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Rita De Zorzi
Matthias R Schmidt
João R C Muniz
Lejla Zubcevic
Mark S P Sansom
Catherine Vénien-Bryan
Stephen J Tucker
University of Oxford · GBClarendon College · USInstitute of Molecular Biology and Biophysics · RU

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BB/F013035/1Biotechnology and Biological Sciences Research Council BB/H000267/1Biotechnology and Biological Sciences Research Council BB/H007296/1Biotechnology and Biological Sciences Research Council BB/I019855/1Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032Wellcome Trust 084655
6 · The paper itself

Abstract

KirBac channels are prokaryotic homologs of mammalian inwardly rectifying (Kir) potassium channels, and recent crystal structures of both Kir and KirBac channels have provided major insight into their unique structural architecture. However, all of the available structures are closed at the helix bundle crossing, and therefore the structural mechanisms that control opening of their primary activation gate remain unknown. In this study, we engineered the inner pore-lining helix (TM2) of KirBac3.1 to trap the bundle crossing in an apparently open conformation and determined the crystal structure of this mutant channel to 3.05 Å resolution. Contrary to previous speculation, this new structure suggests a mechanistic model in which rotational 'twist' of the cytoplasmic domain is coupled to opening of the bundle-crossing gate through a network of inter- and intrasubunit interactions that involve the TM2 C-linker, slide helix, G-loop and the CD loop.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCrystallography, X-RayMagnetospirillumModels, BiologicalModels, MolecularMutant ProteinsMutation, MissensePotassium ChannelsProtein BindingProtein ConformationProtein Structure, TertiaryProtein SubunitsBacterial ProteinsMutant ProteinsPotassium ChannelsProtein Subunits

Identifiers

PMID22231399
PMCPMC3272479
OpenAlexW2103770142

What OpenQuestion holds

Textmetadata
LicenceTDM
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.