Evidence map›Paper›PMID 19701184›Full record

ArticleNature2009

Structure of a tetrameric MscL in an expanded intermediate state.

Zhenfeng Liu, Chris S Gandhi, Douglas C Rees

Abstract read
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed.

  1. Article
  2. When can AlphaFold predict the oligomeric states of proteins?Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Prokaryotic mechanosensitive channels mediate copper influx.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Nanchung and Inactive define pore properties of the native auditory transduction channel inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Pseudomonas doesn't mind a dunking.The Journal of general physiology · 2017
    Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Zhenfeng LiuDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Chris S Gandhi
Douglas C Rees

Funding

Biophysical, Structural and Functional Analysis of Mechanosensitive ChannelsR01GM084211 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HASWELL, ELIZABETH S, PHILLIPS, ROB · 2008 to 2016
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM084211NIGMS NIH HHS R01 GM084211
6 · The paper itself

Abstract

The ability of cells to sense and respond to mechanical force underlies diverse processes such as touch and hearing in animals, gravitropism in plants, and bacterial osmoregulation. In bacteria, mechanosensation is mediated by the mechanosensitive channels of large (MscL), small (MscS), potassium-dependent (MscK) and mini (MscM) conductances. These channels act as 'emergency relief valves' protecting bacteria from lysis upon acute osmotic down-shock. Among them, MscL has been intensively studied since the original identification and characterization 15 years ago. MscL is reversibly and directly gated by changes in membrane tension. In the open state, MscL forms a non-selective 3 nS conductance channel which gates at tensions close to the lytic limit of the bacterial membrane. An earlier crystal structure at 3.5 A resolution of a pentameric MscL from Mycobacterium tuberculosis represents a closed-state or non-conducting conformation. MscL has a complex gating behaviour; it exhibits several intermediates between the closed and open states, including one putative non-conductive expanded state and at least three sub-conducting states. Although our understanding of the closed and open states of MscL has been increasing, little is known about the structures of the intermediate states despite their importance in elucidating the complete gating process of MscL. Here we present the crystal structure of a carboxy-terminal truncation mutant (Delta95-120) of MscL from Staphylococcus aureus (SaMscL(CDelta26)) at 3.8 A resolution. Notably, SaMscL(CDelta26) forms a tetrameric channel with both transmembrane helices tilted away from the membrane normal at angles close to that inferred for the open state, probably corresponding to a non-conductive but partially expanded intermediate state.

Indexed as

Amino Acid SequenceBacterial ProteinsCrystallography, X-RayIon Channel GatingIon ChannelsModels, BiologicalModels, MolecularMolecular Sequence DataMycobacterium tuberculosisPressureProtein Structure, QuaternaryStaphylococcus aureusStructural Homology, ProteinBacterial ProteinsIon Channels

Identifiers

PMID19701184
PMCPMC2737600

What OpenQuestion holds

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Registered trials

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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.