Evidence map›Paper›PMID 23897477›Full record

ArticleActa crystallographica. Section D, Biological crystallography2013

Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ.

Thomas R M Barends, Richard W W Brosi, Andrea Steinmetz, Anna Scherer, Elisabeth Hartmann, Jessica Eschenbach, Thorsten Lorenz, Ralf Seidel, Robert L Shoeman, Sabine Zimmermann and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Overexpression of seagrass DnaJ genePhysiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  8. Article
  9. The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  10. Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein science : a publication of the Protein Society · 2020
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Structure (London, England : 1993) · 2016
    Review
  16. Article
  17. Article
  18. Structural insights into mis-regulation of protein kinase A in human tumors.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

13 authors at 3 institutions in 1 country.

Thomas R M BarendsMPI for Medical Research, Heidelberg, Germany. thomas.barends@mpimf-heidelberg.mpg.de
Richard W W Brosi
Andrea Steinmetz
Anna Scherer
Elisabeth Hartmann
Jessica Eschenbach
Thorsten Lorenz
Ralf Seidel
Robert L Shoeman
Sabine Zimmermann
Robert Bittl
Ilme Schlichting
Jochen Reinstein
Max Planck Institute for Medical Research · DEFreie Universität Berlin · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp70 chaperones assist in a large variety of protein-folding processes in the cell. Crucial for these activities is the regulation of Hsp70 by Hsp40 cochaperones. DnaJ, the bacterial homologue of Hsp40, stimulates ATP hydrolysis by DnaK (Hsp70) and thus mediates capture of substrate protein, but is also known to possess chaperone activity of its own. The first structure of a complete functional dimeric DnaJ was determined and the mobility of its individual domains in solution was investigated. Crystal structures of the complete molecular cochaperone DnaJ from Thermus thermophilus comprising the J, GF and C-terminal domains and of the J and GF domains alone showed an ordered GF domain interacting with the J domain. Structure-based EPR spin-labelling studies as well as cross-linking results showed the existence of multiple states of DnaJ in solution with different arrangements of the various domains, which has implications for the function of DnaJ.

Indexed as

Amino Acid SubstitutionBacterial ProteinsCrystallography, X-RayElectron Spin Resonance SpectroscopyHSP40 Heat-Shock ProteinsMethionineModels, MolecularMolecular ChaperonesProtein ConformationProtein FoldingProtein Structure, TertiaryThermus thermophilusBacterial ProteinsHSP40 Heat-Shock ProteinsMethionineMolecular Chaperonescross-linkingcrystal dehydrationelectron paramagnetic resonancehybrid structure determinationmolecular chaperonesradiation-damage-induced phasing with anomalous scatteringsingle-wavelength anomalous diffraction

Identifiers

PMID23897477
PMCPMC3727329
OpenAlexW2141564795

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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.