Evidence map›Paper›PMID 24486010›Full record

ArticleFEBS letters2014

Crenactin from Pyrobaculum calidifontis is closely related to actin in structure and forms steep helical filaments.

Thierry Izoré, Ramona Duman, Danguole Kureisaite-Ciziene, Jan Löwe

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Archaea and the origin of eukaryotes.Nature reviews. Microbiology · 2017
    Review
  6. Review
  7. Structure of the magnetosome-associated actin-like MamK filament at subnanometer resolution.Protein science : a publication of the Protein Society · 2017
    Article
  8. Article
  9. Article
  10. Review
  11. Origin of eukaryotes from within archaea, archaeal eukaryome and bursts of gene gain: eukaryogenesis just made easier?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  12. In search of the primordial actin filament.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Archaeal actin from a hyperthermophile forms a single-stranded filament.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Thierry IzoréMRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.
Ramona DumanMRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.
Danguole Kureisaite-CizieneMRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom.
Jan LöweMRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom. Electronic address: jyl@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

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

Abstract

Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, are more closely related to actin than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved the crystal structure of crenactin at 3.2 Å resolution. The protein crystallises as a continuous right-handed helix with 8 subunits per complete turn, spanning 419 Å. The structure of crenactin shows several loops that are longer than in actin, but overall, crenactin is closely related to eukaryotic actin, with an RMSD of 1.6 Å. Crenactin filaments imaged by electron microscopy showed polymers with very similar helical parameters.

Indexed as

PyrobaculumActinsArchaeal ProteinsCrystallography, X-RayModels, MolecularPolymerizationProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryStructural Homology, ProteinActinsArchaeal ProteinsActinBacterial cytoskeletonCrenarchaeaCytomotive filamentHelical filamentMreB

Identifiers

PMID24486010
PMCPMC4158420
OpenAlexW2163601999

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.