Evidence map›Paper›PMID 22039461›Full record

ArticlePloS one2011

Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing of 2-oxoglutarate.

Sarah Maier, Paula Schleberger, Wei Lü, Tobias Wacker, Tobias Pflüger, Claudia Litz, Susana L A Andrade

Abstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. The Signal Transduction Protein PFrontiers in microbiology · 2019
    Article
  5. Article
  6. The PFrontiers in molecular biosciences · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. 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

7 authors.

Sarah MaierInstitut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Paula Schleberger
Wei Lü
Tobias Wacker
Tobias Pflüger
Claudia Litz
Susana L A Andrade

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GlnK proteins regulate the active uptake of ammonium by Amt transport proteins by inserting their regulatory T-loops into the transport channels of the Amt trimer and physically blocking substrate passage. They sense the cellular nitrogen status through 2-oxoglutarate, and the energy level of the cell by binding both ATP and ADP with different affinities. The hyperthermophilic euryarchaeon Archaeoglobus fulgidus possesses three Amt proteins, each encoded in an operon with a GlnK ortholog. One of these proteins, GlnK2 was recently found to be incapable of binding 2-OG, and in order to understand the implications of this finding we conducted a detailed structural and functional analysis of a second GlnK protein from A. fulgidus, GlnK3. Contrary to Af-GlnK2 this protein was able to bind both ATP/2-OG and ADP to yield inactive and functional states, respectively. Due to the thermostable nature of the protein we could observe the exact positioning of the notoriously flexible T-loops and explain the binding behavior of GlnK proteins to their interaction partner, the Amt proteins. A thermodynamic analysis of these binding events using microcalorimetry evaluated by microstate modeling revealed significant differences in binding cooperativity compared to other characterized P(II) proteins, underlining the diversity and adaptability of this class of regulatory signaling proteins.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateArchaeal ProteinsArchaeoglobus fulgidusBase SequenceDNA PrimersKetoglutaric AcidsModels, MolecularPolymerase Chain ReactionProtein ConformationAdenosine DiphosphateAdenosine TriphosphateArchaeal ProteinsDNA PrimersKetoglutaric Acids

Identifiers

PMID22039461
PMCPMC3198391

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Registered trials

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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.