Evidence map›Paper›PMID 12065399›Full record

ArticleThe EMBO journal2002

Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA.

Laurence Serre, Karine Pereira de Jésus, Serge Boiteux, Charles Zelwer, Bertrand Castaing

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Alleviation of C⋅C Mismatches in DNA by theFrontiers in microbiology · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Review
  9. Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Strandwise translocation of a DNA glycosylase on undamaged DNA.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage.Progress in molecular biology and translational science · 2012
    Review
  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

5 authors at 1 institution in 1 country.

Laurence SerreInstitut de Biologie Structurale, CNRS-CEA, 41 av. Jules Horowitz, 38027 Grenoble cedex 01, France.
Karine Pereira de Jésus
Serge Boiteux
Charles Zelwer
Bertrand Castaing
CEA Grenoble · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened purines, from oxidatively damaged DNA. The structure of a non-covalent complex between the Lactoccocus lactis Fpg and a 1,3-propanediol (Pr) abasic site analogue-containing DNA has been solved. Through an asymmetric interaction along the damaged strand and the intercalation of the triad (M75/R109/F111), Fpg pushes out the Pr site from the DNA double helix, recognizing the cytosine opposite the lesion and inducing a 60 degrees bend of the DNA. The specific recognition of this cytosine provides some structural basis for understanding the divergence between Fpg and its structural homologue endo nuclease VIII towards their substrate specificities. In addition, the modelling of the 8-oxoguanine residue allows us to define an enzyme pocket that may accommodate the extrahelical oxidized base.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceCrystallography, X-RayDNADNA-Formamidopyrimidine GlycosylaseDNA RepairLactococcus lactisModels, MolecularMolecular Sequence DataMolecular StructureN-Glycosyl HydrolasesProtein BindingSequence AlignmentDNADNA-Formamidopyrimidine GlycosylaseN-Glycosyl Hydrolases

Identifiers

PMID12065399
PMCPMC126059
OpenAlexW2022443227

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.