Evidence map›Paper›PMID 18940922›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.

Cezar M Khursigara, Xiongwu Wu, Peijun Zhang, Jonathan Lefman, Sriram Subramaniam

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.9field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 81 citations in OpenAlex.

  1. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. Recent structural advances in bacterial chemotaxis signalling.Current opinion in structural biology · 2023
    Review
  6. Review
  7. Studying bacterial chemosensory array with CryoEM.Biochemical Society transactions · 2021
    Review
  8. Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021
    Review
  9. Article
  10. Structure and function of the juxtamembrane GAF domain of potassium biosensor KdpD.Protein science : a publication of the Protein Society · 2020
    Article
  11. Article
  12. Review
  13. Propulsion and Chemotaxis in Bacteria-Driven Microswimmers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2017
    Article
  14. Information processing in bacteria: memory, computation, and statistical physics: a key issues review.Reports on progress in physics. Physical Society (Great Britain) · 2016
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 at 4 institutions in 1 country.

Cezar M KhursigaraLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Xiongwu Wu
Peijun Zhang
Jonathan Lefman
Sriram Subramaniam
National Cancer Institute · USNational Heart Lung and Blood Institute · USNational Institutes of Health · USUniversity of Pittsburgh · US

Funding

Molecular structures of membrane protein assembliesZIABC010824 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Molecular structure of the bacterial chemotaxis apparatusZ01BC010824 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2007 to 2008
$1.1M
Intramural NIH HHS
6 · The paper itself

Abstract

Bacterial chemoreceptors undergo conformational changes in response to variations in the concentration of extracellular ligands. These changes in chemoreceptor structure initiate a series of signaling events that ultimately result in regulation of rotation of the flagellar motor. Here we have used cryo-electron tomography combined with 3D averaging to determine the in situ structure of chemoreceptor assemblies in Escherichia coli cells that have been engineered to overproduce the serine chemoreceptor Tsr. We demonstrate that chemoreceptors are organized as trimers of receptor dimers and display two distinct conformations that differ principally in arrangement of the HAMP domains within each trimer. Ligand binding and methylation alter the distribution of chemoreceptors between the two conformations, with serine binding favoring the "expanded" conformation and chemoreceptor methylation favoring the "compact" conformation. The distinct positions of chemoreceptor HAMP domains within the context of a trimeric unit are thus likely to represent important aspects of chemoreceptor structural changes relevant to chemotaxis signaling. Based on these results, we propose that the compact and expanded conformations represent the "kinase-on" and "kinase-off" states of chemoreceptor trimers, respectively.

Indexed as

ChemotaxisSignal TransductionBacterial ProteinsChemoreceptor CellsEscherichia coliEscherichia coli ProteinsLigandsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMethylationMultiprotein ComplexesPhosphotransferasesProtein BindingProtein Structure, TertiaryBacterial ProteinsEscherichia coli ProteinsLigandsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMultiprotein ComplexesPhosphotransferasestsr protein, E coli

Identifiers

PMID18940922
PMCPMC2570609
OpenAlexW2000050637

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.