Evidence map›Paper›PMID 15359276›Full record

ArticleThe EMBO journal2004

Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis.

Sigrun Rumpel, Adelia Razeto, Chris M Pillar, Vinesh Vijayan, Austin Taylor, Karin Giller, Michael S Gilmore, Stefan Becker, Markus Zweckstetter

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Bibacillin 1: A two-component lantibiotic frombioRxiv : the preprint server for biology · 2024
    Article
  5. An Overview of the Factors Involved in Biofilm Production by theInternational journal of molecular sciences · 2023
    Review
  6. Infection and drug resistance · 2023
    Article
  7. Anti-Biofilm and Antibacterial Activities ofAntibiotics (Basel, Switzerland) · 2022
    Article
  8. Article
  9. Article
  10. Enterococcal Genetics.Microbiology spectrum · 2019
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  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

9 authors at 2 institutions in 2 countries.

Sigrun RumpelDepartment for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Adelia Razeto
Chris M Pillar
Vinesh Vijayan
Austin Taylor
Karin Giller
Michael S Gilmore
Stefan Becker
Markus Zweckstetter
Max Planck Institute for Biophysical Chemistry · DEUniversity of Oklahoma Health Sciences Center · US

Funding

TOXINS AND ENDOPHTHALMITISR01EY008289 · NEI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI GILMORE, MICHAEL S, GREGORY-KSANDER, MEREDITH · 1989 to 2012
$3.7M
NOVEL ENTEROCOCCAL TOXIN--REGULATION OF EXPRESSIONR01AI041108 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI GILMORE, MICHAEL S · 1998 to 2007
$2.5M
NEI NIH HHS EY08289NEI NIH HHS R01 EY008289NIAID NIH HHS AI41108NIAID NIH HHS R01 AI041108
6 · The paper itself

Abstract

Enterococcus faecalis is one of the major causes for hospital-acquired antibiotic-resistant infections. It produces an exotoxin, called cytolysin, which is lethal for a wide range of Gram-positive bacteria and is toxic to higher organisms. Recently, the regulation of the cytolysin operon was connected to autoinduction by a quorum-sensing mechanism involving the CylR1/CylR2 two-component regulatory system. We report here the crystal structure of CylR2 and its properties in solution as determined by heteronuclear NMR spectroscopy. The structure reveals a rigid dimer containing a helix-turn-helix DNA-binding motif as part of a five-helix bundle that is extended by an antiparallel beta-sheet. We show that CylR2 is a DNA-binding protein that binds specifically to a 22 bp fragment of the cytolysin promoter region. NMR chemical shift perturbation experiments identify surfaces involved in DNA binding and are in agreement with a model for the CylR2/DNA complex that attributes binding specificity to a complex network of CylR2/DNA interactions. Our results propose a mechanism where repression is achieved by CylR2 obstruction of the promoter preventing biosynthesis of the cytolysin operon transcript.

Indexed as

Bacterial ProteinsBacteriocinsBinding SitesCrystallography, X-RayDimerizationDNA-Binding ProteinsEnterococcus faecalisGene Expression Regulation, BacterialHelix-Turn-Helix MotifsMagnetic Resonance SpectroscopyModels, MolecularOperonPromoter Regions, GeneticProtein BindingProtein ConformationRepressor ProteinsBacterial ProteinsBacteriocinscytolysin, Enterococcus faecalisDNA-Binding ProteinsRepressor Proteins

Identifiers

PMID15359276
PMCPMC517608
OpenAlexW2160616401

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.