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Chaperone PDB id
1bq0
Jmol
Contents
Protein chain
77 a.a. *
* Residue conservation analysis
PDB id:
1bq0
Name: Chaperone
Title: J-domain (residues 1-77) of the escherichia coli n-terminal fragment (residues 1-104) of the molecular chaperone dnaj, nmr, 20 structures
Structure: Dnaj. Chain: a. Fragment: n-terminal fragment (residues 1-104). Synonym: hsp40. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: K.Huang,J.M.Flanagan,J.H.Prestegard
Key ref:
K.Huang et al. (1999). The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ. Protein Sci, 8, 203-214. PubMed id: 10210198 Ref: Full text
Date:
20-Aug-98     Release date:   15-Jun-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P08622  (DNAJ_ECOLI) -  Chaperone protein DnaJ
Seq:
Struc: 		376 a.a.
77 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   1 term 
  Biochemical function     heat shock protein binding     2 terms  

 

 
Full text Protein Sci 8:203-214 (1999)
PubMed id: 10210198  
 
 
The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ.
K.Huang, J.M.Flanagan, J.H.Prestegard.
 
  ABSTRACT  
 
Two different recombinant constructs of the N-terminal domain in Escherichia coli DnaJ were uniformly labeled with nitrogen-15 and carbon-13. One, DnaJ(1-78), contains the complete "J-domain," and the other, DnaJ(1-104), contains both the "J-domain" and a conserved "G/F" extension at the C-terminus. The three-dimensional structures of these proteins have been determined by heteronuclear NMR experiments. In both proteins the "J-domain" adopts a compact structure consisting of a helix-turn-helix-loop-helix-turn-helix motif. In contrast, the "G/F" region in DnaJ(1-104) does not fold into a well-defined structure. Nevertheless, the "G/F" region has been found to have an effect on the packing of the helices in the "J-domain" in DnaJ(1-104). Particularly, the interhelical angles between Helix IV and other helices are significantly different in the two structures. In addition, there are some local conformational changes in the loop region connecting the two central helices. These structural differences in the "J-domain" in the presence of the "G/F" region may be related to the observation that DnaJ (1-78) is incapable of stimulating the ATPase activity of the molecular chaperone protein DnaK despite evidence that sites mediating the binding of DnaJ to DnaK are located in the 1-78 segment.
 
  Selected figure(s)  
 
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (1999, 8, 203-214) copyright 1999.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20487283 J.M.Cloward, and D.C.Krause (2010).
Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ.
  Mol Microbiol, 77, 158-169.  
18022798 K.Khalili, I.K.Sariyer, and M.Safak (2008).
Small tumor antigen of polyomaviruses: role in viral life cycle and cell transformation.
  J Cell Physiol, 215, 309-319.  
17239655 W.S.Nicoll, M.Botha, C.McNamara, M.Schlange, E.R.Pesce, A.Boshoff, M.H.Ludewig, R.Zimmermann, M.E.Cheetham, J.P.Chapple, and G.L.Blatch (2007).
Cytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK.
  Int J Biochem Cell Biol, 39, 736-751.  
15687271 R.Aron, N.Lopez, W.Walter, E.A.Craig, and J.Johnson (2005).
In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae.
  Genetics, 169, 1873-1882.  
15273304 J.M.Gruschus, L.E.Greene, E.Eisenberg, and J.A.Ferretti (2004).
Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural change.
  Protein Sci, 13, 2029-2044.  
15704013 W.A.McLaughlin, D.W.Kulp, J.de la Cruz, X.J.Lu, C.L.Lawson, and H.M.Berman (2004).
A structure-based method for identifying DNA-binding proteins and their sites of DNA-interaction.
  J Struct Funct Genomics, 5, 255-265.  
12718534 S.J.Landry (2003).
Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK.
  Biochemistry, 42, 4926-4936.  
12040123 C.S.Sullivan, and J.M.Pipas (2002).
T antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesis.
  Microbiol Mol Biol Rev, 66, 179-202.  
11226179 H.Y.Kim, B.Y.Ahn, and Y.Cho (2001).
Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen.
  EMBO J, 20, 295-304.
PDB code: 1gh6
11257542 S.Al-Herran, and W.Ashraf (2001).
The immunological dissection of the Escherichia coli molecular chaperone DnaJ.
  FEMS Microbiol Lett, 196, 19-23.  
  10523664 W.Yan, and E.A.Craig (1999).
The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1.
  Mol Cell Biol, 19, 7751-7758.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.