Evidence map›Paper›PMID 25092919›Full record

ArticleNucleic acids research2014

Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2).

Hussain Bhukya, Ruchika Bhujbalrao, Aruna Bitra, Ruchi Anand

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Biochemistry · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. The regulatory cascades of antibiotic production in Streptomyces.World journal of microbiology & biotechnology · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. 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

4 authors.

Hussain BhukyaDepartment of Chemistry, Indian Institute of Technology Bombay, Mumbai 400076, Maharashtra, India IITB-Monash Research Academy, Mumbai 400076, Maharashtra, India.
Ruchika BhujbalraoDepartment of Chemistry, Indian Institute of Technology Bombay, Mumbai 400076, Maharashtra, India.
Aruna BitraDepartment of Chemistry, Indian Institute of Technology Bombay, Mumbai 400076, Maharashtra, India.
Ruchi AnandDepartment of Chemistry, Indian Institute of Technology Bombay, Mumbai 400076, Maharashtra, India ruchi@chem.iitb.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibiotic production and resistance pathways in Streptomyces are dictated by the interplay of transcriptional regulatory proteins that trigger downstream responses via binding to small diffusible molecules. To decipher the mode of DNA binding and the associated allosteric mechanism in the sub-class of transcription factors that are induced by γ-butyrolactones, we present the crystal structure of CprB in complex with the consensus DNA element to a resolution of 3.25 Å. Binding of the DNA results in the restructuring of the dimeric interface of CprB, inducing a pendulum-like motion of the helix-turn-helix motif that inserts into the major groove. The crystal structure revealed that, CprB is bound to DNA as a dimer of dimers with the mode of binding being analogous to the broad spectrum multidrug transporter protein QacR from the antibiotic resistant strain Staphylococcus aureus. It was demonstrated that the CprB displays a cooperative mode of DNA binding, following a clamp and click model. Experiments performed on a subset of DNA sequences from Streptomyces coelicolor A3(2) suggest that CprB is most likely a pleiotropic regulator. Apart from serving as an autoregulator, it is potentially a part of a network of proteins that modulates the γ-butyrolactone synthesis and antibiotic regulation pathways in S. coelicolor A3(2).

Indexed as

ApoproteinsBacterial ProteinsBase SequenceConsensus SequenceDNA, BacterialDNA-Binding ProteinsGene Expression Regulation, BacterialModels, MolecularMutagenesisProtein BindingProtein MultimerizationProtein Structure, TertiaryStreptomyces coelicolorTranscription FactorsTranscription, GeneticApoproteinsBacterial ProteinsDNA, BacterialDNA-Binding ProteinsTranscription Factors

Identifiers

PMID25092919
PMCPMC4150764

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.