Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ

J Mol Biol. 2000 Jul 21;300(4):805-18. doi: 10.1006/jmbi.2000.3923.


The solution structure of the cysteine-rich (CR) domain of Escherichia coli DnaJ has been solved by NMR methods. The structure of a 79 residue CR domain construct shows a novel fold with an overall V-shaped extended beta-hairpin topology. The CR domain is characterized by four C-X-X-C-X-G-X-G sequence motifs that bind two zinc ions. Residues in these two zinc modules show strong similarities in the grouping of resonances in the (15)N-(1)H HSQC spectrum and display pseudo-symmetry of the motifs in the calculated structures. The conformation of the cysteine residues coordinated to the zinc ion resembles that of the rubredoxin-knuckle, but there are significant differences in hydrogen bonding patterns in the two motifs. Zinc (15)N-(1)H HSQC titrations indicate that the fold of the isolated DnaJ CR domain is zinc-dependent and that one zinc module folds before the other. The C-X-X-C-X-G-X-G sequence motif is highly conserved in CR domains from a wide variety of species. The three-dimensional structure of the E. coli CR domain indicates that this sequence conservation is likely to result in a conserved structural motif.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Conserved Sequence
  • Cysteine / chemistry
  • Cysteine / metabolism*
  • Escherichia coli / chemistry*
  • Escherichia coli Proteins
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides / metabolism
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Solutions
  • Zinc / metabolism


  • Bacterial Proteins
  • DnaJ protein, E coli
  • Escherichia coli Proteins
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Peptides
  • Solutions
  • Zinc
  • Cysteine

Associated data

  • PDB/1EXK