Evidence map›Paper›PMID 18593706›Full record

ArticleThe Journal of biological chemistry2008

Crystal structure of the lysine riboswitch regulatory mRNA element.

Andrew D Garst, Annie Héroux, Robert P Rambo, Robert T Batey

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

119 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
  2. Article
  3. ACS chemical biology · 2025
    Article
  4. Ligand-binding pockets in RNA and where to find them.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. A Riboswitch-Driven Era of New Antibacterials.Antibiotics (Basel, Switzerland) · 2022
    Review
  15. Article
  16. In-Cell NMR Spectroscopy of Functional Riboswitch Aptamers in Eukaryotic Cells.Angewandte Chemie (International ed. in English) · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article

59 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Andrew D GarstDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, Boulder, Colorado 80309, USA.
Annie Héroux
Robert P Rambo
Robert T Batey
University of Colorado Boulder · USBrookhaven National Laboratory · USLawrence Berkeley National Laboratory · US

Funding

Basis of Gene Regulation by Purine-Binding mRNAsR01GM073850 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI BATEY, ROBERT T · 2005 to 2022
$4.8M
NIGMS NIH HHS GM073850
6 · The paper itself

Abstract

Riboswitches are metabolite-sensitive elements found in mRNAs that control gene expression through a regulatory secondary structural switch. Along with regulation of lysine biosynthetic genes, mutations within the lysine-responsive riboswitch (L-box) play a role in the acquisition of resistance to antimicrobial lysine analogs. To understand the structural basis for lysine binding, we have determined the 2.8 angstroms resolution crystal structure of lysine bound to the Thermotoga maritima asd lysine riboswitch ligand-binding domain. The structure reveals a complex architecture scaffolding a binding pocket completely enveloping lysine. Mutations conferring antimicrobial resistance cluster around this site as well as highly conserved long range interactions, indicating that they disrupt lysine binding or proper folding of the RNA. Comparison of the free and bound forms by x-ray crystallography, small angle x-ray scattering, and chemical probing reveals almost identical structures, indicating that lysine induces only limited and local conformational changes upon binding.

Indexed as

LysineCrystallography, X-RayDNA, BacterialLigandsMagnesiumModels, MolecularMolecular Sequence DataNucleic Acid ConformationRNA, BacterialRNA, MessengerThermotoga maritimaDNA, BacterialLigandsLysineMagnesiumRNA, BacterialRNA, Messenger

Identifiers

PMID18593706
PMCPMC2504901
OpenAlexW2070293903

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.