Evidence map›Paper›PMID 29323112›Full record

ArticleNature communications2018

Signaling ammonium across membranes through an ammonium sensor histidine kinase.

Tobias Pflüger, Camila F Hernández, Philipp Lewe, Fabian Frank, Haydyn Mertens, Dmitri Svergun, Manfred W Baumstark, Vladimir Y Lunin, Mike S M Jetten, Susana L A Andrade

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  14. Synthetic cells in biomedical applications.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022
    Review
  15. Role of protein phosphatases in the regulation of nitrogen nutrition in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Review
  16. Review
  17. Sensor Domain of Histidine Kinase VxrA ofJournal of bacteriology · 2021
    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

10 authors at 4 institutions in 3 countries.

Tobias PflügerInstitute for Biochemistry, University of Freiburg, Albertstr. 21, Freiburg, 79104, Germany.
Camila F HernándezInstitute for Biochemistry, University of Freiburg, Albertstr. 21, Freiburg, 79104, Germany.
Philipp LeweInstitute for Biochemistry, University of Freiburg, Albertstr. 21, Freiburg, 79104, Germany.
Fabian FrankInstitute for Biochemistry, University of Freiburg, Albertstr. 21, Freiburg, 79104, Germany.
Haydyn MertensEuropean Molecular Biology Laboratory, Hamburg Unit, EMBL c/o DESY, Notkestr. 85, Hamburg, D-22603, Germany.ORCID http://orcid.org/0000-0002-5664-744X
Dmitri SvergunEuropean Molecular Biology Laboratory, Hamburg Unit, EMBL c/o DESY, Notkestr. 85, Hamburg, D-22603, Germany.
Manfred W BaumstarkCenter for Medicine, Institute for Exercise and Occupational Medicine, Medical Center, University of Freiburg, Hugstetterstr. 55, Freiburg, 79106, Germany.
Vladimir Y LuninInstitute of Mathematical Problems of Biology RAS, Keldysh Institute of Applied Mathematics of Russian Academy of Sciences, Vitkevicha str. 1, Pushchino, 142290, Russia.ORCID http://orcid.org/0000-0003-1235-1206
Mike S M JettenDepartment of Microbiology, Radboud University, Institute for Water and Wetland Research, Heyendaalseweg 135, Nijmegen, NL-6525 AJ, The Netherlands.
Susana L A AndradeInstitute for Biochemistry, University of Freiburg, Albertstr. 21, Freiburg, 79104, Germany. andrade@bio.chemie.uni-freiburg.de.
University of Freiburg · DEEuropean Molecular Biology Laboratory · DEInstitute of Mathematical Problems of Biology · RURadboud University Nijmegen · NL

Funding

European Research Council 024002002European Research Council 232937European Research Council 339880
6 · The paper itself

Abstract

Sensing and uptake of external ammonium is essential for anaerobic ammonium-oxidizing (anammox) bacteria, and is typically the domain of the ubiquitous Amt/Rh ammonium transporters. Here, we report on the structure and function of an ammonium sensor/transducer from the anammox bacterium "Candidatus Kuenenia stuttgartiensis" that combines a membrane-integral ammonium transporter domain with a fused histidine kinase. It contains a high-affinity ammonium binding site not present in assimilatory Amt proteins. The levels of phosphorylated histidine in the kinase are coupled to the presence of ammonium, as conformational changes during signal recognition by the Amt module are transduced internally to modulate the kinase activity. The structural analysis of this ammonium sensor by X-ray crystallography and small-angle X-ray-scattering reveals a flexible, bipartite system that recruits a large uptake transporter as a sensory module and modulates its functionality to achieve a mechanistic coupling to a kinase domain in order to trigger downstream signaling events.

Indexed as

Signal TransductionAmino Acid SequenceAmmonium CompoundsBacteriaBacterial ProteinsBinding SitesCell MembraneCrystallography, X-RayHistidine KinaseMembrane Transport ProteinsModels, MolecularOxidation-ReductionProtein BindingProtein DomainsScattering, Small AngleSequence Homology, Amino AcidAmmonium CompoundsBacterial ProteinsHistidine KinaseMembrane Transport Proteins

Identifiers

PMID29323112
PMCPMC5764959
OpenAlexW2782464043

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.