Evidence map›Paper›PMID 19952067›Full record

ArticleNucleic acids research2010

Dynamics of the base of ribosomal A-site finger revealed by molecular dynamics simulations and Cryo-EM.

Kamila Réblová, Filip Rázga, Wen Li, Haixiao Gao, Joachim Frank, Jirí Sponer

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. The translation elongation cycle-capturing multiple states by cryo-electron microscopy.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  6. Intersubunit Bridges of the Bacterial Ribosome.Journal of molecular biology · 2016
    Review
  7. Stacking in RNA: NMR of Four Tetramers Benchmark Molecular Dynamics.Journal of chemical theory and computation · 2015
    Article
  8. Article
  9. Initial bridges between two ribosomal subunits are formed within 9.4 milliseconds, as studied by time-resolved cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. Article
  12. Intermediate states during mRNA-tRNA translocation.Current opinion in structural biology · 2012
    Review
  13. Article
  14. Computational studies of molecular machines: the ribosome.Current opinion in structural biology · 2012
    Review
  15. Article
  16. Article
  17. Article
  18. 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

6 authors at 1 institution in 1 country.

Kamila RéblováInstitute of Biophysics, Academy of Sciences of the Czech Republic, Kralovopolská 135, 61265 Brno, Czech Republic.
Filip Rázga
Wen Li
Haixiao Gao
Joachim Frank
Jirí Sponer
Czech Academy of Sciences · CZ

Funding

Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01GM55440
6 · The paper itself

Abstract

Helix 38 (H38) of the large ribosomal subunit, with a length of 110 A, reaches the small subunit through intersubunit bridge B1a. Previous cryo-EM studies revealed that the tip of H38 moves by more than 10 A from the non-ratcheted to the ratcheted state of the ribosome while mutational studies implicated a key role of flexible H38 in attenuation of translocation and in dynamical signaling between ribosomal functional centers. We investigate a region including the elbow-shaped kink-turn (Kt-38) in the Haloarcula marismortui archaeal ribosome, and equivalently positioned elbows in three eubacterial species, located at the H38 base. We performed explicit solvent molecular dynamics simulations on the H38 elbows in all four species. They are formed by at first sight unrelated sequences resulting in diverse base interactions but built with the same overall topology, as shown by X-ray crystallography. The elbows display similar fluctuations and intrinsic flexibilities in simulations indicating that the eubacterial H38 elbows are structural and dynamical analogs of archaeal Kt-38. We suggest that this structural element plays a pivotal role in the large motions of H38 and may act as fulcrum for the abovementioned tip motion. The directional flexibility inferred from simulations correlates well with the cryo-EM results.

Indexed as

Cryoelectron MicroscopyDeinococcusEscherichia coliHaloarcula marismortuiMolecular Dynamics SimulationNucleic Acid ConformationPotassium ChlorideRibosome Subunits, Large, ArchaealRibosome Subunits, Large, BacterialRNA, Ribosomal, 23SSodiumThermus thermophilusPotassium ChlorideRNA, Ribosomal, 23SSodium

Identifiers

PMID19952067
PMCPMC2831300
OpenAlexW1972845513

What OpenQuestion holds

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LicenceCC BY-NC
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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.