Evidence map›Paper›PMID 24843005›Full record

ArticleeLife2014

Bacterial actin MreB forms antiparallel double filaments.

Fusinita van den Ent, Thierry Izoré, Tanmay Am Bharat, Christopher M Johnson, Jan Löwe

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
12.6field-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

102 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Bacterial actin MreB as a new antibiotic target.Frontiers in molecular biosciences · 2026
    Article
  5. Article
  6. Live imaging of bacterial actin MreBs fromBiophysics and physicobiology · 2026
    Article
  7. Sensing the shape of a surface by tightly surface-bound filaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Improving Stability ofBio-protocol · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

42 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

5 authors at 2 institutions in 1 country.

Fusinita van den EntStructural Studies Division, Medical Research Council - Laboratory of Molecular Biology, Cambridge, United Kingdom fent@mrc-lmb.cam.ac.uk.
Thierry IzoréStructural Studies Division, Medical Research Council - Laboratory of Molecular Biology, Cambridge, United Kingdom.
Tanmay Am BharatStructural Studies Division, Medical Research Council - Laboratory of Molecular Biology, Cambridge, United Kingdom.
Christopher M JohnsonProtein and Nucleic Acid Chemistry Division, Medical Research Council - Laboratory of Molecular Biology, Cambridge, United Kingdom.
Jan LöweStructural Studies Division, Medical Research Council - Laboratory of Molecular Biology, Cambridge, United Kingdom.
MRC Laboratory of Molecular Biology · GBMedical Research Council · GB

Funding

Medical Research Council MC_U105184326Medical Research Council U105184326Wellcome Trust 095514Wellcome Trust 095514/Z/11/Z
6 · The paper itself

Abstract

Filaments of all actin-like proteins known to date are assembled from pairs of protofilaments that are arranged in a parallel fashion, generating polarity. In this study, we show that the prokaryotic actin homologue MreB forms pairs of protofilaments that adopt an antiparallel arrangement in vitro and in vivo. We provide an atomic view of antiparallel protofilaments of Caulobacter MreB as apparent from crystal structures. We show that a protofilament doublet is essential for MreB's function in cell shape maintenance and demonstrate by in vivo site-specific cross-linking the antiparallel orientation of MreB protofilaments in E. coli. 3D cryo-EM shows that pairs of protofilaments of Caulobacter MreB tightly bind to membranes. Crystal structures of different nucleotide and polymerisation states of Caulobacter MreB reveal conserved conformational changes accompanying antiparallel filament formation. Finally, the antimicrobial agents A22/MP265 are shown to bind close to the bound nucleotide of MreB, presumably preventing nucleotide hydrolysis and destabilising double protofilaments.DOI: http://dx.doi.org/10.7554/eLife.02634.001.

Indexed as

Actin CytoskeletonActinsBacterial ProteinsCaulobacter crescentusCross-Linking ReagentsCrystallography, X-RayCysteineEscherichia coliHumansLipidsModels, MolecularMutationNanotubesNucleotidesPolymerizationProtein BindingActinsBacterial ProteinsCross-Linking ReagentsCysteineLipidsNucleotidesbacteriaCaulobacter crescentusThermotoga maritima

Identifiers

PMID24843005
PMCPMC4051119
OpenAlexW2100819048

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.