Evidence map›Paper›PMID 24526190›Full record

ArticleNature communications2014

An asymmetric heterodomain interface stabilizes a response regulator-DNA complex.

Anoop Narayanan, Shivesh Kumar, Amanda N Evrard, Lake N Paul, Dinesh A Yernool

Abstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Regulatory role ofFrontiers in microbiology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. TheFrontiers in microbiology · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Characterization of FtsH Essentiality inFrontiers in genetics · 2021
    Article
  18. Article
  19. Structure and function of the juxtamembrane GAF domain of potassium biosensor KdpD.Protein science : a publication of the Protein Society · 2020
    Article
  20. Frontiers in cellular and infection microbiology · 2020
    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

5 authors.

Anoop Narayanan1] Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA [2].
Shivesh Kumar1] Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA [2] [3].
Amanda N EvrardDepartment of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA.
Lake N PaulBindley Bioscience Center, Purdue University, 1203 West State Street, West Lafayette, Indiana 47907, USA.
Dinesh A Yernool1] Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA [2] Bindley Bioscience Center, Purdue University, 1203 West State Street, West Lafayette, Indiana 47907, USA.

Funding

Structure and Function of Sodium-Calcium ExchangersR01GM093142 · NIGMS · PURDUE UNIVERSITY · PI YERNOOL, DINESH A · 2011 to 2015
$1.4M
NIGMS NIH HHS R01 GM093142
6 · The paper itself

Abstract

Two-component signal transduction systems consist of pairs of histidine kinases and response regulators, which mediate adaptive responses to environmental cues. Most activated response regulators regulate transcription by binding tightly to promoter DNA via a phosphorylation-triggered inactive-to-active transition. The molecular basis for formation of stable response regulator-DNA complexes that precede the assembly of RNA polymerases is unclear. Here, we present structures of DNA complexed with the response regulator KdpE, a member of the OmpR/PhoB family. The distinctively asymmetric complex in an active-like conformation reveals a unique intramolecular interface between the receiver domain (RD) and the DNA-binding domain (DBD) of only one of the two response regulators in the complex. Structure-function studies show that this RD-DBD interface is necessary to form stable complexes that support gene expression. The conservation of sequence and structure suggests that these findings extend to a large group of response regulators that act as transcription factors.

Indexed as

DNAEscherichia coliEscherichia coli ProteinsProtein ConformationStructure-Activity RelationshipTrans-ActivatorsDNAEscherichia coli ProteinskdpE protein, E coliTrans-Activators

Identifiers

PMID24526190
PMCPMC4399498

What OpenQuestion holds

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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.