Evidence map›Paper›PMID 20435045›Full record

ArticleJournal of molecular biology2010

Structural characterization of the predominant family of histidine kinase sensor domains.

Zhen Zhang, Wayne A Hendrickson

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

67 citing papers in PubMed, 125 citations in OpenAlex.

  1. Functional Characterization ofPlants (Basel, Switzerland) · 2026
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  3. A Model of the Full-Length Cytokinin Receptor: New Insights and Prospects.International journal of molecular sciences · 2023
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  4. Amine-recognizing domain in diverse receptors from bacteria and archaea evolved from the universal amino acid sensor.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  13. The role of solute binding proteins in signal transduction.Computational and structural biotechnology journal · 2021
    Review
  14. Interface switch mediates signal transmission in a two-component system.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  17. The type IV pilin PilA couples surface attachment and cell-cycle initiation inProceedings of the National Academy of Sciences of the United States of America · 2020
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7 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Zhen ZhangHoward Hughes Medical Institute, Columbia University, New York, NY 10032, USA.
Wayne A Hendrickson
Columbia University · US

Funding

ANOMALOUS-SCATTERING STUDIES OF MACROMOLECULAR STRUCTURER37GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1994 to 2003
$1.4M
ANOMALOUS-SCATTERING STUDIES OF PROTEIN STRUCTURER01GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1985 to 2008
$1.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM34102NIGMS NIH HHS R01 GM034102NIGMS NIH HHS R37 GM034102
6 · The paper itself

Abstract

Histidine kinase (HK) receptors are used ubiquitously by bacteria to monitor environmental changes, and they are also prevalent in plants, fungi, and other protists. Typical HK receptors have an extracellular sensor portion that detects a signal, usually a chemical ligand, and an intracellular transmitter portion that includes both the kinase domain itself and the site for histidine phosphorylation. While kinase domains are highly conserved, sensor domains are diverse. HK receptors function as dimers, but the molecular mechanism for signal transduction across cell membranes remains obscure. In this study, eight crystal structures were determined from five sensor domains representative of the most populated family, family HK1, found in a bioinformatic analysis of predicted sensor domains from transmembrane HKs. Each structure contains an inserted repeat of PhoQ/DcuS/CitA (PDC) domains, and similarity between sequence and structure is correlated across these and other double-PDC sensor proteins. Three of the five sensors crystallize as dimers that appear to be physiologically relevant, and comparisons between ligated structures and apo-state structures provide insights into signal transmission. Some HK1 family proteins prove to be sensors for chemotaxis proteins or diguanylate cyclase receptors, implying a combinatorial molecular evolution.

Indexed as

Amino Acid SequenceCrystallography, X-RayDimerizationHistidine KinaseMethanosarcinaModels, MolecularMolecular Sequence DataProtein ConformationProtein KinasesProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRhodopseudomonasSequence AlignmentShewanellaVibrio parahaemolyticusHistidine KinaseProtein Kinases

Identifiers

PMID20435045
PMCPMC3461309
OpenAlexW2161178127

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.