Evidence map›Paper›PMID 23012406›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy.

Christos Pliotas, Richard Ward, Emma Branigan, Akiko Rasmussen, Gregor Hagelueken, Hexian Huang, Susan S Black, Ian R Booth, Olav Schiemann, James H Naismith

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
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

51 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. PELDOR Measurements on Nitroxide-Labeled Oligonucleotides.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Spin Labeling of Long RNAs Via Click Reaction and Enzymatic Ligation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  17. Article
  18. Mechanosensitive channel gating by delipidation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Article
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

10 authors.

Christos PliotasBiomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews KY16 9ST, United Kingdom.
Richard Ward
Emma Branigan
Akiko Rasmussen
Gregor Hagelueken
Hexian Huang
Susan S Black
Ian R Booth
Olav Schiemann
James H Naismith

Funding

Biotechnology and Biological Sciences Research Council BB/H017402/1Biotechnology and Biological Sciences Research Council BB/H017917/1Wellcome Trust 092552Wellcome Trust WT092552MA
6 · The paper itself

Abstract

The heptameric mechanosensitive channel of small conductance (MscS) provides a critical function in Escherichia coli where it opens in response to increased bilayer tension. Three approaches have defined different closed and open structures of the channel, resulting in mutually incompatible models of gating. We have attached spin labels to cysteine mutants on key secondary structural elements specifically chosen to discriminate between the competing models. The resulting pulsed electron-electron double resonance (PELDOR) spectra matched predicted distance distributions for the open crystal structure of MscS. The fit for the predictions by structural models of MscS derived by other techniques was not convincing. The assignment of MscS as open in detergent by PELDOR was unexpected but is supported by two crystal structures of spin-labeled MscS. PELDOR is therefore shown to be a powerful experimental tool to interrogate the conformation of transmembrane regions of integral membrane proteins.

Indexed as

Models, MolecularProtein ConformationBlotting, WesternChromatography, GelCrystallographyElectron Spin Resonance SpectroscopyEscherichia coli ProteinsIon ChannelsMutagenesisPatch-Clamp TechniquesSequence Analysis, DNASpectrum AnalysisSpin LabelsEscherichia coli ProteinsIon ChannelsMscS protein, E coliSpin Labels

Identifiers

PMID23012406
PMCPMC3479538

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.