Evidence map›Paper›PMID 16319927›Full record

ArticleThe EMBO journal2005

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein.

Alberto Marina, Carey D Waldburger, Wayne A Hendrickson

Abstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing 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

154 citing papers in PubMed.

  1. Genomic analysis highlights a novel class of DPCF-type cyanobacteriochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
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  13. A Model of the Full-Length Cytokinin Receptor: New Insights and Prospects.International journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

94 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

3 authors.

Alberto MarinaHoward Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Carey D Waldburger
Wayne A Hendrickson

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
MOLECULAR MECHANISMS OF PHOP-PHOQ SIGNAL TRANSDUCTIONR01AI041566 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CAREY, WALDBURGER DUANE · 1997 to 2001
$476k
NIAID NIH HHS AI41566NIGMS NIH HHS GM34102NIGMS NIH HHS R01 GM034102NIGMS NIH HHS R37 GM034102
6 · The paper itself

Abstract

The large majority of histidine kinases (HKs) are multifunctional enzymes having autokinase, phosphotransfer and phosphatase activities, and most of these are transmembrane sensor proteins. Sensor HKs possess conserved cytoplasmic phosphorylation and ATP-binding kinase domains. The different enzymatic activities require participation by one or both of these domains, implying the need for different conformational states. The catalytic domains are linked to the membrane through a coiled-coil segment that sometimes includes other domains. We describe here the first crystal structure of the complete cytoplasmic region of a sensor HK, one from the thermophile Thermotoga maritima in complex with ADPbetaN at 1.9 A resolution. The structure reveals previously unidentified functions for several conserved residues and reveals the relative disposition of domains in a state seemingly poised for phosphotransfer. The structure thereby inspires hypotheses for the mechanisms of autophosphorylation, phosphotransfer and response-regulator dephosphorylation, and for signal transduction through the coiled-coil segment. Mutational tests support the functional relevance of interdomain contacts.

Indexed as

Adenosine TriphosphateAmino Acid SequenceBinding SitesCloning, MolecularCrystallography, X-RayCytoplasmDimerizationDNA Mutational AnalysisEscherichia coliHistidineHistidine KinaseModels, MolecularMolecular Sequence DataMutationPhosphorylationProtein BindingAdenosine TriphosphateHistidineHistidine KinaseProtein Kinases

Identifiers

PMID16319927
PMCPMC1356327

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.