Evidence map›Paper›PMID 19422057›Full record

ArticleProteins2009

Solution structure of the DNA binding domain of AraC protein.

Michael E Rodgers, Robert Schleif

Abstract read
In one paragraph

Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. The CpxR-GlvR regulatory axis ofFrontiers in cellular and infection microbiology · 2026
    Article
  2. Article
  3. A Twist of Fate: The Helix-Turn-Helix Motif inJournal of chemical information and modeling · 2025
    Article
  4. Phase Separation to Resolve Growth-Related Circuit Failures.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Optimised Heterologous Expression and Functional Analysis of theInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Analysis of amino acid substitutions in AraC variants that respond to triacetic acid lactone.Protein science : a publication of the Protein Society · 2016
    Article
  15. Review
  16. Article
  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

2 authors.

Michael E RodgersBiology Department, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Robert Schleif

Funding

REGULATORY MECHANISMS OF THE E COLI ARABINOSE OPERONR37GM018277 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHLEIF, ROBERT F. · 1994 to 2004
$2.3M
REGULATORY MECHANISMS OF THE E COLI ARABINOSE OPERONR01GM018277 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHLEIF, ROBERT F. · 1985 to 2009
$2.2M
BIOPHYSICS OF THE NUCLEOPROTEIN ACCESSORY PROTEIN NHP6AF32GM018277 · NIGMS · FOX CHASE CANCER CENTER · PI KATZ, DARIN S · 1996 to 1997
–
NIGMS NIH HHS F32 GM018277NIGMS NIH HHS GM18277NIGMS NIH HHS R01 GM018277NIGMS NIH HHS R37 GM018277
6 · The paper itself

Abstract

We report the solution structure of the DNA binding domain of the Escherichia coli regulatory protein AraC determined in the absence of DNA. The 20 lowest energy structures, determined on the basis of 1507 unambiguous nuclear Overhauser restraints and 180 angle restraints, are well resolved with a pair wise backbone root mean square deviation of 0.7 A. The protein, free of DNA, is well folded in solution and contains seven helices arranged in two semi-independent sub domains, each containing one helix-turn-helix DNA binding motif, joined by a 19 residue central helix. This solution structure is discussed in the context of extensive biochemical and physiological data on AraC and with respect to the DNA-bound structures of the MarA and Rob homologs.

Indexed as

AraC Transcription FactorDNAEscherichia coli ProteinsMagnetic Resonance SpectroscopyModels, BiologicalProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryAraC Transcription FactorDNAEscherichia coli Proteins

Identifiers

PMID19422057
PMCPMC2745637

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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.