Evidence map›Paper›PMID 16243784›Full record

ArticleNucleic acids research2005

Structural insights into abasic site for Fpg specific binding and catalysis: comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNA.

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

Open access · goldAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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
  6. Article
  7. DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. The Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damage.Progress in molecular biology and translational science · 2012
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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.

Karine Pereira de JésusCentre de Biophysique Moléculaire, CNRS rue Charles Sadron, 45071 Orléans cedex 02, France.
Laurence Serre
Charles Zelwer
Bertrand Castaing
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fpg is a DNA glycosylase that recognizes and excises the mutagenic 8-oxoguanine (8-oxoG) and the potentially lethal formamidopyrimidic residues (Fapy). Fpg is also associated with an AP lyase activity which successively cleaves the abasic (AP) site at the 3' and 5' sides by betadelta-elimination. Here, we present the high-resolution crystal structures of the wild-type and the P1G defective mutant of Fpg from Lactococcus lactis bound to 14mer DNA duplexes containing either a tetrahydrofuran (THF) or 1,3-propanediol (Pr) AP site analogues. Structures show that THF is less extrahelical than Pr and its backbone C5'-C4'-C3' diverges significantly from those of Pr, rAP, 8-oxodG and FapydG. Clearly, the heterocyclic oxygen of THF is pushed back by the carboxylate of the strictly conserved E2 residue. We can propose that the ring-opened form of the damaged deoxyribose is the structure active form of the sugar for Fpg catalysis process. Both structural and functional data suggest that the first step of catalysis mediated by Fpg involves the expulsion of the O4' leaving group facilitated by general acid catalysis (involving E2), rather than the immediate cleavage of the N-glycosic bond of the damaged nucleoside.

Indexed as

Models, MolecularBacterial ProteinsBinding SitesCatalysisCrystallography, X-RayDNADNA DamageDNA-Formamidopyrimidine GlycosylaseFuransLactococcus lactisMutationPropylene Glycols1,3-propanediolBacterial ProteinsDNADNA-Formamidopyrimidine GlycosylaseFuransPropylene Glycolstetrahydrofuran

Identifiers

PMID16243784
PMCPMC1266061
OpenAlexW2149305996

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.