Evidence map›Paper›PMID 28498104›Full record

ArticleeLife2017

Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis.

Duccio Malinverni, Alfredo Jost Lopez, Paolo De Los Rios, Gerhard Hummer, Alessandro Barducci

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. The J Domain Proteins ofInternational journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. CISD3/MiNT is required for complex I function, mitochondrial integrity, and skeletal muscle maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Review
  8. Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Review
  9. Article
  10. Article
  11. TheFrontiers in molecular biosciences · 2023
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  20. 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

5 authors at 4 institutions in 3 countries.

Duccio MalinverniLaboratoire de Biophysique Statistique, Faculté de Sciences de Base, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Alfredo Jost LopezMax Planck Institute of Biophysics, Frankfurt am Main, Germany.
Paolo De Los RiosLaboratoire de Biophysique Statistique, Faculté de Sciences de Base, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.ORCID 0000-0002-5394-5062
Gerhard HummerMax Planck Institute of Biophysics, Frankfurt am Main, Germany.
Alessandro BarducciInserm, U1054, Montpellier, France.ORCID 0000-0002-1911-8039
École Polytechnique Fédérale de Lausanne · CHCentre National de la Recherche Scientifique · FRGoethe University Frankfurt · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction between the Heat Shock Proteins 70 and 40 is at the core of the ATPase regulation of the chaperone machinery that maintains protein homeostasis. However, the structural details of the interaction remain elusive and contrasting models have been proposed for the transient Hsp70/Hsp40 complexes. Here we combine molecular simulations based on both coarse-grained and atomistic models with coevolutionary sequence analysis to shed light on this problem by focusing on the bacterial DnaK/DnaJ system. The integration of these complementary approaches resulted in a novel structural model that rationalizes previous experimental observations. We identify an evolutionarily conserved interaction surface formed by helix II of the DnaJ J-domain and a structurally contiguous region of DnaK, involving lobe IIA of the nucleotide binding domain, the inter-domain linker, and the β-basket of the substrate binding domain.

Indexed as

Protein Interaction MapsEscherichia coli ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular Dynamics SimulationProtein BindingSequence AnalysisDnaJ protein, E colidnaK protein, E coliEscherichia coli ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock Proteinsbiophysicscomputational biologyheat shock proteinmolecular modelingnoneprotein coevolutionprotein complexstructural biologysystems biologytransient interaction

Identifiers

PMID28498104
PMCPMC5519331
OpenAlexW2522058963

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.