Evidence map›Paper›PMID 22028633›Full record

ArticlePLoS computational biology2011

Transmembrane helix dynamics of bacterial chemoreceptors supports a piston model of signalling.

Benjamin A Hall, Judith P Armitage, Mark S P Sansom

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 43 citations in OpenAlex.

  1. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. A chemoreceptor conformational equilibrium controlled by signaling inputs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Activation of the bacterial thermosensor DesK involves a serine zipper dimerization motif that is modulated by bilayer thickness.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Review
  19. Article
  20. Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

3 authors at 1 institution in 1 country.

Benjamin A HallOxford Centre for Integrative Systems Biology, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Judith P Armitage
Mark S P Sansom
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BB/H000267/1Biotechnology and Biological Sciences Research Council BB/I019855/1Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032
6 · The paper itself

Abstract

Transmembrane α-helices play a key role in many receptors, transmitting a signal from one side to the other of the lipid bilayer membrane. Bacterial chemoreceptors are one of the best studied such systems, with a wealth of biophysical and mutational data indicating a key role for the TM2 helix in signalling. In particular, aromatic (Trp and Tyr) and basic (Arg) residues help to lock α-helices into a membrane. Mutants in TM2 of E. coli Tar and related chemoreceptors involving these residues implicate changes in helix location and/or orientation in signalling. We have investigated the detailed structural basis of this via high throughput coarse-grained molecular dynamics (CG-MD) of Tar TM2 and its mutants in lipid bilayers. We focus on the position (shift) and orientation (tilt, rotation) of TM2 relative to the bilayer and how these are perturbed in mutants relative to the wildtype. The simulations reveal a clear correlation between small (ca. 1.5 Å) shift in position of TM2 along the bilayer normal and downstream changes in signalling activity. Weaker correlations are seen with helix tilt, and little/none between signalling and helix twist. This analysis of relatively subtle changes was only possible because the high throughput simulation method allowed us to run large (n = 100) ensembles for substantial numbers of different helix sequences, amounting to ca. 2000 simulations in total. Overall, this analysis supports a swinging-piston model of transmembrane signalling by Tar and related chemoreceptors.

Indexed as

Molecular Dynamics SimulationSignal TransductionAmino Acid SequenceEscherichia coliEscherichia coli ProteinsMembrane ProteinsMolecular Sequence DataMutationProtein Structure, SecondaryReceptors, Cell SurfaceEscherichia coli ProteinsMembrane ProteinsReceptors, Cell Surface

Identifiers

PMID22028633
PMCPMC3197627
OpenAlexW2075004481

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.