Evidence map›Paper›PMID 19928961›Full record

ArticleJournal of the American Chemical Society2009

Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor.

Zhen Ma, Darin M Cowart, Brian P Ward, Randy J Arnold, Richard D DiMarchi, Limei Zhang, Graham N George, Robert A Scott, David P Giedroc

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Review
  2. Article
  3. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. TheThe Journal of biological chemistry · 2019
    Article
  9. Article
  10. Allosteric histidine switch for regulation of intracellular zinc(II) fluctuation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  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

9 authors.

Zhen MaDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405-7102, USA.
Darin M Cowart
Brian P Ward
Randy J Arnold
Richard D DiMarchi
Limei Zhang
Graham N George
Robert A Scott
David P Giedroc

Funding

ZINC COORDINATION AND REGULATION OF ZINC METALLOPROTEINSR01GM042569 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 1996 to 2015
$4.9M
TRAININGP41RR018942 · NCRR · TRUSTEES OF INDIANA UNIVERSITY · PI REILLY, JAMES P. · 2005 to 2008
$3.9M
X-RAY ABSORPTION SPECTROSCOPY OF METALLOENZYMESR01GM042025 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI SCOTT, ROBERT A · 1989 to 2010
$2.6M
ZINC DOMAIN STRUCTURE AND FUNCTION IN T4 GENE 32 PROTEINR29GM042569 · NIGMS · TEXAS AGRILIFE RESEARCH · PI GIEDROC, DAVID P. · 1991 to 1995
–
CIHRNCRR NIH HHS P41 RR018942NIGMS NIH HHS GM042025NIGMS NIH HHS GM042569NIGMS NIH HHS R01 GM042025NIGMS NIH HHS R01 GM042569
6 · The paper itself

Abstract

The Cu(I) sensor Mycobacterium tuberculosis CsoR is a founding member of a new metalloregulatory protein family. Here we show that two "atom" substitutions of the Nepsilon2 face of a Cu(I) coordinating histidine-61 allosterically uncouple Cu(I) and DNA binding, with no effect on Cu(I) binding affinity and coordination structure. A model analogous to the allosteric switch mechanism in Staphylococcus aureus CzrA, a zinc sensor protein with a completely different fold, is proposed.

Indexed as

Amino Acid SubstitutionAllosteric RegulationAllosteric SiteBacterial ProteinsCopperDNA-Binding ProteinsHistidineHydrogen BondingModels, MolecularMycobacterium tuberculosisBacterial ProteinsCopperCsoR protein, Mycobacterium tuberculosisDNA-Binding ProteinsHistidine

Identifiers

PMID19928961
PMCPMC2797707

What OpenQuestion holds

Textmetadata
LicenceTDM
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.