Evidence map›Paper›PMID 31992852›Full record

ArticleCommunications biology2020

Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.

Matthew Jessop, Benoit Arragain, Roger Miras, Angélique Fraudeau, Karine Huard, Maria Bacia-Verloop, Patrice Catty, Jan Felix, Hélène Malet, Irina Gutsche

Abstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
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  13. AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021
    Review
  14. Article
  15. Supramolecular assembly of theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. AAA+ proteins: converging mechanisms, diverging functions.Nature structural & molecular biology · 2020
    Article
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.

Matthew Jessop *Institut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France.ORCID http://orcid.org/0000-0001-8880-4481
Benoit Arragain *Institut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France.ORCID http://orcid.org/0000-0002-5593-4682
Roger MirasLaboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, CEA, CNRS, DRF, IRIG, UMR 5249, 17 rue des Martyrs, F-38054, Grenoble, France.
Angélique FraudeauInstitut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France.
Karine HuardInstitut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France.
Maria Bacia-VerloopInstitut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France.
Patrice CattyLaboratoire de Chimie et Biologie des Métaux, Univ. Grenoble Alpes, CEA, CNRS, DRF, IRIG, UMR 5249, 17 rue des Martyrs, F-38054, Grenoble, France.
Jan FelixInstitut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France. jan.felix@ibs.fr.ORCID http://orcid.org/0000-0002-8436-9467
Hélène MaletInstitut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France. helene.malet@ibs.fr.ORCID http://orcid.org/0000-0002-2834-7386
Irina GutscheInstitut de Biologie Structurale, Univ. Grenoble Alpes, CEA, CNRS, IBS, 71 Avenue des martyrs, F-38044, Grenoble, France. irina.gutsche@ibs.fr.ORCID http://orcid.org/0000-0002-1908-3921

Funding

European Molecular Biology Organization (EMBO) ALTF441-2017
6 · The paper itself

Abstract

The hexameric MoxR AAA+ ATPase RavA and the decameric lysine decarboxylase LdcI form a 3.3 MDa cage, proposed to assist assembly of specific respiratory complexes in E. coli. Here, we show that inside the LdcI-RavA cage, RavA hexamers adopt an asymmetric spiral conformation in which the nucleotide-free seam is constrained to two opposite orientations. Cryo-EM reconstructions of free RavA reveal two co-existing structural states: an asymmetric spiral, and a flat C2-symmetric closed ring characterised by two nucleotide-free seams. The closed ring RavA state bears close structural similarity to the pseudo two-fold symmetric crystal structure of the AAA+ unfoldase ClpX, suggesting a common ATPase mechanism. Based on these structures, and in light of the current knowledge regarding AAA+ ATPases, we propose different scenarios for the ATP hydrolysis cycle of free RavA and the LdcI-RavA cage-like complex, and extend the comparison to other AAA+ ATPases of clade 7.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateCarboxy-LyasesCatalytic DomainCryoelectron MicroscopyCrystallizationCrystallography, X-RayElectron Transport Complex IEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationHydrolysisProtein BindingProtein Conformation, alpha-HelicalAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateCarboxy-LyasesElectron Transport Complex IEscherichia coli Proteinslysine decarboxylaseRavA protein, E coli

Identifiers

PMID31992852
PMCPMC6987120

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.