Evidence map›Paper›PMID 21911405›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Crystal structure of QscR, a Pseudomonas aeruginosa quorum sensing signal receptor.

Mario J Lintz, Ken-ichi Oinuma, Christina L Wysoczynski, Everett Peter Greenberg, Mair E A Churchill

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

69 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. MrtR ofProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Assessing the antibacterial potential of 6-gingerol: Combined experimental and computational approaches.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
    Article
  11. Thymoquinone is a natural antibiofilm and pathogenicity attenuating agent inFrontiers in cellular and infection microbiology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Anti-quorum sensing activity ofBioinformation · 2023
    Article
  19. Article
  20. Article

9 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

5 authors at 2 institutions in 1 country.

Mario J LintzDepartment of Pharmacology, Structural Biology and Biophysics Program, University of Colorado Denver School of Medicine, Aurora, CO 80045, USA.
Ken-ichi Oinuma
Christina L Wysoczynski
Everett Peter Greenberg
Mair E A Churchill
University of Colorado Denver · USUniversity of Washington · US

Funding

QUORUM SENSING IN PSEUDOMONAS AERUGINOSAR01GM059026 · NIGMS · UNIVERSITY OF WASHINGTON · PI GREENBERG, EVERETT P · 1999 to 2019
$6.5M
Molecular Basis of Bacterial Quorum Sensing Gene RegulationR56AI081872 · NIAID · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 2010 to 2010
$404k
Howard Hughes Medical InstituteNIAID NIH HHS R56 AI081872NIAID NIH HHS R56AI081872NIGMS NIH HHS R01 GM059026NIGMS NIH HHS R01GM59026
6 · The paper itself

Abstract

Acyl-homoserine lactone (AHL) quorum sensing controls gene expression in hundreds of Proteobacteria including a number of plant and animal pathogens. Generally, the AHL receptors are members of a family of related transcription factors, and although they have been targets for development of antivirulence therapeutics there is very little structural information about this class of bacterial receptors. We have determined the structure of the transcription factor, QscR, bound to N-3-oxo-dodecanoyl-homoserine lactone from the opportunistic human pathogen Pseudomonas aeruginosa at a resolution of 2.55 Å. The ligand-bound QscR is a dimer with a unique symmetric "cross-subunit" arrangement containing multiple dimerization interfaces involving both domains of each subunit. The QscR dimer appears poised to bind DNA. Predictions about signal binding and dimerization contacts were supported by studies of mutant QscR proteins in vivo. The acyl chain of the AHL is in close proximity to the dimerization interfaces. Our data are consistent with an allosteric mechanism of signal transmission in the regulation of DNA binding and thus virulence gene expression.

Indexed as

Quorum SensingAcyl-ButyrolactonesAmino Acid SequenceBacterial ProteinsBase SequenceBinding SitesCircular DichroismCrystallizationCrystallography, X-RayDNA, BacterialHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationAcyl-ButyrolactonesBacterial ProteinsDNA, BacterialQscR protein, Pseudomonas aeruginosaRepressor Proteins

Identifiers

PMID21911405
PMCPMC3179110
OpenAlexW2162160645

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.