Evidence map›Paper›PMID 27455459›Full record

ArticleNature structural & molecular biology2016

Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi.

Sebastian Glatt, Rene Zabel, Olga Kolaj-Robin, Osita F Onuma, Florence Baudin, Andrea Graziadei, Valerio Taverniti, Ting-Yu Lin, Frauke Baymann, Bertrand Seraphin and 2 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Microbiology spectrum · 2026
    Article
  4. Transcription Factors in Plant Gene Expression Regulation.International journal of molecular sciences · 2025
    Article
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  7. Review
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  15. Article
  16. Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022
    Review
  17. Review
  18. Review
  19. AtELP4 a subunit of the Elongator complex inFrontiers in plant science · 2022
    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

12 authors at 4 institutions in 3 countries.

Sebastian GlattEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Rene Zabel *Institute of Biology, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany.
Olga Kolaj-Robin *Université de Strasbourg, IGBMC UMR 7104, Illkirch, France.
Osita F OnumaInstitute of Biology, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany.
Florence BaudinEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Andrea GraziadeiEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Valerio TavernitiUniversité de Strasbourg, IGBMC UMR 7104, Illkirch, France.
Ting-Yu LinMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
Frauke BaymannLaboratoire de Bioénergétique et Ingénierie des Protéines, BIP/CNRS, UMR7281, AMU, Marseille, France.
Bertrand SeraphinUniversité de Strasbourg, IGBMC UMR 7104, Illkirch, France.
Karin D BreunigInstitute of Biology, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany.
Christoph W MüllerEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Centre National de la Recherche Scientifique · FRMartin Luther University Halle-Wittenberg · DEEuropean Molecular Biology Laboratory · DEJagiellonian University · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During translation elongation, decoding is based on the recognition of codons by corresponding tRNA anticodon triplets. Molecular mechanisms that regulate global protein synthesis via specific base modifications in tRNA anticodons are receiving increasing attention. The conserved eukaryotic Elongator complex specifically modifies uridines located in the wobble base position of tRNAs. Mutations in Elongator subunits are associated with certain neurodegenerative diseases and cancer. Here we present the crystal structure of D. mccartyi Elp3 (DmcElp3) at 2.15-Å resolution. Our results reveal an unexpected arrangement of Elp3 lysine acetyltransferase (KAT) and radical S-adenosyl methionine (SAM) domains, which share a large interface and form a composite active site and tRNA-binding pocket, with an iron-sulfur cluster located in the dimerization interface of two DmcElp3 molecules. Structure-guided mutagenesis studies of yeast Elp3 confirmed the relevance of our findings for eukaryotic Elp3s and should aid in understanding the cellular functions and pathophysiological roles of Elongator.

Indexed as

Bacterial ProteinsCatalytic DomainChloroflexiCrystallography, X-RayHistone AcetyltransferasesProtein BindingProtein Conformation, alpha-HelicalProtein MultimerizationRNA, BacterialRNA, TransferSubstrate SpecificityBacterial ProteinsHistone AcetyltransferasesRNA, BacterialRNA, Transfer

Identifiers

PMID27455459
PMCPMC5018218
OpenAlexW2479147916

What OpenQuestion holds

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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.