4J80

Thermus thermophilus DnaJ


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.265 
  • R-Value Observed: 0.267 

    wwPDB Validation   3D Report Full Report


    This is version 1.1 of the entry. See complete history


    Literature

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

    Barends, T.R.Brosi, R.W.Steinmetz, A.Scherer, A.Hartmann, E.Eschenbach, J.Lorenz, T.Seidel, R.Shoeman, R.L.Zimmermann, S.Bittl, R.Schlichting, I.Reinstein, J.

    (2013) Acta Crystallogr D Biol Crystallogr 69: 1540-1552

    • DOI: https://doi.org/10.1107/S0907444913010640
    • Primary Citation of Related Structures:  
      4J7Z, 4J80

    • PubMed 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.


    • Organizational Affiliation

      MPI for Medical Research, Heidelberg, Germany. thomas.barends@mpimf-heidelberg.mpg.de


    Macromolecules
    Find similar proteins by:  (by identity cutoff)  |  3D Structure
    Entity ID: 1
    MoleculeChains Sequence LengthOrganismDetailsImage
    Chaperone protein DnaJ 2
    A, B, C, D
    284Thermus thermophilus HB8Mutation(s): 5 
    Gene Names: dnaJ2TTHA1489
    UniProt
    Find proteins for Q56237 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
    Explore Q56237 
    Go to UniProtKB:  Q56237
    Entity Groups  
    Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
    UniProt GroupQ56237
    Sequence Annotations
    Expand
    • Reference Sequence
    Small Molecules
    Modified Residues  1 Unique
    IDChains TypeFormula2D DiagramParent
    MSE
    Query on MSE
    A, B, C, D
    L-PEPTIDE LINKINGC5 H11 N O2 SeMET
    Experimental Data & Validation

    Experimental Data

    • Method: X-RAY DIFFRACTION
    • Resolution: 2.90 Å
    • R-Value Free: 0.307 
    • R-Value Work: 0.265 
    • R-Value Observed: 0.267 
    • Space Group: P 21 21 2
    Unit Cell:
    Length ( Å )Angle ( ˚ )
    a = 102.09α = 90
    b = 105β = 90
    c = 130.03γ = 90
    Software Package:
    Software NamePurpose
    ADSCdata collection
    SHARPphasing
    REFMACrefinement
    XDSdata reduction
    XSCALEdata scaling

    Structure Validation

    View Full Validation Report



    Entry History 

    Revision History  (Full details and data files)

    • Version 1.0: 2013-07-31
      Type: Initial release
    • Version 1.1: 2013-10-09
      Changes: Database references