Evidence map›Paper›PMID 27081063›Full record

ArticleScience (New York, N.Y.)2016

Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.

Erica L Schwalm, Tyler L Grove, Squire J Booker, Amie K Boal

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.2field-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

50 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026
    Article
  4. Review
  5. Structural Basis for CbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
  11. CNature communications · 2024
    Article
  12. Review
  13. Cluster-selectiveChemical science · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022
    Review
  18. Review
  19. Article
  20. Structure of a BNature · 2022
    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.

Erica L SchwalmDepartment of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.
Tyler L GroveDepartment of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.
Squire J BookerDepartment of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA. Howard Hughes Medical Institute, Pennsylvania State University, University Park, PA 16802, USA. squire@psu.edu akb20@psu.edu.
Amie K BoalDepartment of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA. squire@psu.edu akb20@psu.edu.
Pennsylvania State University · US

Funding

Mechanisms of Radical-Dependent Biological MethylationR01GM101957 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOOKER, SQUIRE J. · 2012 to 2015
$1.0M
Structure determination of reaction intermediates in macromolecular complexesR00GM100011 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOAL, AMIE K · 2013 to 2015
$729k
Structure determination of reaction intermediates in macromolecular complexesK99GM100011 · NIGMS · NORTHWESTERN UNIVERSITY · PI BOAL, AMIE K · 2012 to 2013
$110k
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS GM100011NIGMS NIH HHS GM101957NIGMS NIH HHS K99 GM100011NIGMS NIH HHS R00 GM100011NIGMS NIH HHS R01 GM101957NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

RlmN is a dual-specificity RNA methylase that modifies C2 of adenosine 2503 (A2503) in 23S rRNA and C2 of adenosine 37 (A37) in several Escherichia coli transfer RNAs (tRNAs). A related methylase, Cfr, modifies C8 of A2503 via a similar mechanism, conferring resistance to multiple classes of antibiotics. Here, we report the x-ray structure of a key intermediate in the RlmN reaction, in which a Cys(118)→Ala variant of the protein is cross-linked to a tRNA(Glu)substrate through the terminal methylene carbon of a formerly methylcysteinyl residue and C2 of A37. RlmN contacts the entire length of tRNA(Glu), accessing A37 by using an induced-fit strategy that completely unfolds the tRNA anticodon stem-loop, which is likely critical for recognition of both tRNA and ribosomal RNA substrates.

Indexed as

AdenosineAlanineAmino Acid SubstitutionAnticodonCatalytic DomainCrystallography, X-RayCysteineEscherichia coli ProteinsMethylationMethyltransferasesNucleic Acid ConformationProtein Structure, TertiaryRNA, BacterialRNA, Transfer, GluS-AdenosylmethionineAdenosineAlanineAnticodonCysteineEscherichia coli ProteinsMethyltransferasesRlmN protein, E coliRNA, BacterialRNA, Transfer, GluS-Adenosylmethionine

Identifiers

PMID27081063
PMCPMC5629962
OpenAlexW2337134136

What OpenQuestion holds

Textmetadata
LicenceTDM
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.