Evidence map›Paper›PMID 19783821›Full record

ArticleNucleic acids research2009

Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition.

Bernhard Loll, Maike Gebhardt, Elmar Wahle, Anton Meinhart

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Role of Bacterial and Host DNases on Host-Pathogen Interaction duringInternational journal of molecular sciences · 2020
    Article
  10. Article
  11. Anti-ROR1 scFv-EndoG as a Novel Anti-Cancer Therapeutic DrugAsian Pacific journal of cancer prevention : APJCP · 2018
    Article
  12. Immunology and Genetic ofJournal of research in medical sciences : the official journal of Isfahan University of Medical Sciences · 2018
    Review
  13. Article
  14. Article
  15. Dnases in health and disease.Developmental biology · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. Structural characterization of the virulence factor nuclease A from Streptococcus agalactiae.Acta crystallographica. Section D, Biological crystallography · 2014
    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

4 authors at 3 institutions in 1 country.

Bernhard LollDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
Maike Gebhardt
Elmar Wahle
Anton Meinhart
Max Planck Institute for Medical Research · DEMartin Luther University Halle-Wittenberg · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EndoG is a ubiquitous nuclease that is translocated into the nucleus during apoptosis to participate in DNA degradation. The enzyme cleaves double- and single-stranded DNA and RNA. Related nucleases are found in eukaryotes and prokaryotes, which have evolved sophisticated mechanisms for genome protection against self-antagonizing nuclease activity. Common mechanisms of inhibition are secretion, sequestration into a separate cellular compartment or by binding to protein inhibitors. Although EndoG is silenced by compartmentalization into the mitochondrial intermembrane space, a nucleus-localized protein inhibitor protects cellular polynucleotides from degradation by stray EndoG under non-apoptotic conditions in Drosophila. Here, we report the first three-dimensional structure of EndoG in complex with its inhibitor EndoGI. Although the mechanism of inhibition is reminiscent of bacterial protein inhibitors, EndoGI has evolved independently from a generic protein-protein interaction module. EndoGI is a two-domain protein that binds the active sites of two monomers of EndoG, with EndoG being sandwiched between EndoGI. Since the amino acid sequences of eukaryotic EndoG homologues are highly conserved, this model is valid for eukaryotic dimeric EndoG in general. The structure indicates that the two active sites of EndoG occupy the most remote spatial position possible at the molecular surface and a concerted substrate processing is unlikely.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalytic DomainConserved SequenceCrystallographyDimerizationDrosophila melanogasterDrosophila ProteinsEndodeoxyribonucleasesEnzyme InhibitorsModels, MolecularMolecular Sequence DataOligonucleotidesDrosophila ProteinsEndodeoxyribonucleasesendonuclease GEnzyme InhibitorsOligonucleotides

Identifiers

PMID19783821
PMCPMC2790893
OpenAlexW2040943384

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.