Evidence map›Paper›PMID 11877432›Full record

ArticleThe Journal of biological chemistry2002

Crystal structure of Thermotoga maritima 0065, a member of the IclR transcriptional factor family.

Rong-Guang Zhang, Youngchang Kim, Tatiana Skarina, Steven Beasley, Roman Laskowski, Cheryl Arrowsmith, Aled Edwards, Andrzej Joachimiak, Alexei Savchenko

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

25 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Molecular control of gene expression byThe Journal of biological chemistry · 2018
    Article
  6. Crystal structure of an IclR homologue from Microbacterium sp. strain HM58-2.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  7. Article
  8. Article
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  18. Structural characterization of GntR/HutC family signaling domain.Protein science : a publication of the Protein Society · 2006
    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 4 institutions in 3 countries.

Rong-Guang ZhangBiosciences Division and Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439, USA.
Youngchang Kim
Tatiana Skarina
Steven Beasley
Roman Laskowski
Cheryl Arrowsmith
Aled Edwards
Andrzej Joachimiak
Alexei Savchenko
Argonne National Laboratory · USUniversity Health Network · CAUniversity of Toronto · CABirkbeck, University of London · GB

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
NIGMS NIH HHS GM62414NIGMS NIH HHS P50 GM062414
6 · The paper itself

Abstract

Members of the IclR family of transcription regulators modulate signal-dependent expression of genes involved in carbon metabolism in bacteria and archaea. The Thermotoga maritima TM0065 gene codes for a protein (TM-IclR) that is homologous to the IclR family. We have determined the crystal structure of TM-IclR at 2.2 A resolution using MAD phasing and synchrotron radiation. The protein is composed of two domains: the N-terminal DNA-binding domain contains the winged helix-turn-helix motif, and the C-terminal presumed regulatory domain is involved in binding signal molecule. In a proposed signal-binding site, a bound Zn(2+) ion was found. In the crystal, TM-IclR forms a dimer through interactions between DNA-binding domains. In the dimer, the DNA-binding domains are 2-fold related, but the dimer is asymmetric with respect to the orientation of signal-binding domains. Crystal packing analysis showed that TM-IclR dimers form a tetramer through interactions exclusively by signal-binding domains. A model is proposed for binding of IclR-like factors to DNA, and it suggests that signal-dependent transcription regulation is accomplished by affecting an oligomerization state of IclR and therefore its affinity for DNA target.

Indexed as

Escherichia coli ProteinsTranscription FactorsAmino Acid SequenceBacterial ProteinsBase SequenceBinding SitesCloning, MolecularCrystallography, X-RayDNA, BacterialModels, MolecularMolecular Sequence DataOpen Reading FramesRepressor ProteinsSequence Homology, Amino AcidThermotoga maritimaBacterial ProteinsDNA, BacterialEscherichia coli ProteinsIclR protein, E coliRepressor ProteinsTranscription Factors

Identifiers

PMID11877432
PMCPMC2792004
OpenAlexW2147108293

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.