Evidence map›Paper›PMID 25097238›Full record

ArticleeLife2014

Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.

Hélène Malet, Kaiyin Liu, Majida El Bakkouri, Sze Wah Samuel Chan, Gregory Effantin, Maria Bacia, Walid A Houry, Irina Gutsche

Erratum issuedAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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. A cloaked glutamate decarboxylase sustains the GABA shunt inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Supramolecular assembly of theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors.

Hélène MaletEuropean Molecular Biology Laboratory, Grenoble, France Unit for Virus Host-Cell Interactions, Université Grenoble Alpes, Grenoble, France Unit for Virus Host-Cell Interactions, CNRS, Grenoble, France.
Kaiyin LiuDepartment of Biochemistry, University of Toronto, Toronto, Canada.
Majida El BakkouriDepartment of Biochemistry, University of Toronto, Toronto, Canada.
Sze Wah Samuel ChanDepartment of Biochemistry, University of Toronto, Toronto, Canada.
Gregory EffantinUnit for Virus Host-Cell Interactions, Université Grenoble Alpes, Grenoble, France Unit for Virus Host-Cell Interactions, CNRS, Grenoble, France.
Maria BaciaUniversité Grenoble Alpes, Institut de Biologie Structurale, Grenoble, France Institut de Biologie Structurale, CNRS, Grenoble, France Institut de Biologie Structurale, CEA, Grenoble, France.
Walid A HouryDepartment of Biochemistry, University of Toronto, Toronto, Canada walid.houry@utoronto.ca.
Irina GutscheUnit for Virus Host-Cell Interactions, Université Grenoble Alpes, Grenoble, France Unit for Virus Host-Cell Interactions, CNRS, Grenoble, France gutsche@embl.fr.

Funding

Canadian Institutes of Health Research MOP-130374
6 · The paper itself

Abstract

A 3.3 MDa macromolecular cage between two Escherichia coli proteins with seemingly incompatible symmetries-the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI-is reconstructed by cryo-electron microscopy to 11 Å resolution. Combined with a 7.5 Å resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily.

Indexed as

Adenosine TriphosphatasesCarboxy-LyasesCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsGene ExpressionModels, MolecularMutationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationRecombinant ProteinsAdenosine TriphosphatasesCarboxy-LyasesEscherichia coli Proteinslysine decarboxylaseRavA protein, E coliRecombinant ProteinsAAA+ ATPaseelectron microscopyimage analysislysine decarboxylasemacromolecular assemblyRavA

Identifiers

PMID25097238
PMCPMC4145799

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.