Evidence map›Paper›PMID 9799245›Full record

ArticleThe EMBO journal1998

The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.

M Stoldt, J Wöhnert, M Görlach, L R Brown

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Evaluation ofJournal of biomolecular NMR · 2017
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  8. The role of structural bioinformatics resources in the era of integrative structural biology.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  9. The natural history of ubiquitin and ubiquitin-related domains.Frontiers in bioscience (Landmark edition) · 2012
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. An intermolecular base triple as the basis of ligand specificity and affinity in the guanine- and adenine-sensing riboswitch RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  16. Article
  17. Article
  18. 5 S rRNA: structure and interactions.The Biochemical journal · 2003
    Review
  19. Role of ctc from Listeria monocytogenes in osmotolerance.Applied and environmental microbiology · 2003
    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

4 authors at 1 institution in 1 country.

M StoldtAbteilung Molekulare Biophysik/NMR Spektroskopie, Institut für Molekulare Biotechnologie e. V., Postfach 100813, 07708 Jena, Germany.
J Wöhnert
M Görlach
L R Brown
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of the Escherichia coli ribosomal protein L25 has been determined to an r.m.s. displacement of backbone heavy atoms of 0.62 +/- 0.14 A by multi-dimensional heteronuclear NMR spectroscopy on protein samples uniformly labeled with 15N or 15N/13C. L25 shows a new topology for RNA-binding proteins consisting of a six-stranded beta-barrel and two alpha-helices. A putative RNA-binding surface for L25 has been obtained by comparison of backbone 15N chemical shifts for L25 with and without a bound cognate RNA containing the eubacterial E-loop that is the site for binding of L25 to 5S ribosomal RNA. Sequence comparisons with related proteins, including the general stress protein, CTC, show that the residues involved in RNA binding are highly conserved, thereby providing further confirmation of the binding surface. Tertiary structure comparisons indicate that the six-stranded beta-barrels of L25 and of the tRNA anticodon-binding domain of glutaminyl-tRNA synthetase are similar.

Indexed as

Amino Acid SequenceAmino Acyl-tRNA SynthetasesBacterial ProteinsBinding SitesEscherichia coliHeat-Shock ProteinsMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein Structure, SecondaryProtein Structure, TertiaryRibosomal ProteinsRNA-Binding ProteinsRNA, Ribosomal, 5SSequence Homology, Amino AcidAmino Acyl-tRNA SynthetasesBacterial Proteinsglutaminyl-tRNA synthetaseHeat-Shock Proteinsribosomal protein L25Ribosomal ProteinsRNA-Binding ProteinsRNA, Ribosomal, 5S

Identifiers

PMID9799245
PMCPMC1170962
OpenAlexW1977932250

What OpenQuestion holds

Textmetadata
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.