NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction

Biochemistry. 1998 Jun 2;37(22):7929-40. doi: 10.1021/bi9800855.


The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision of 1.00 A (backbone of the beta-domain) from 1075 experimental restraints obtained from multinuclear, multidimensional NMR experiments. The domain is observed to bind to its own C-terminus and offers a preview of the interaction of this chaperone with other proteins. The bound protein region is tightly held at a single amino acid position (a leucyl residue) that is buried in a deep pocket lined with conserved hydrophobic residues. A second hydrophobic binding site was identified using paramagnetically labeled peptides. It is located in a region close to the N-terminus of the domain and may constitute the allosteric region that links substrate-binding affinity with nucleotide binding in the Hsp70 chaperones.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Computer Simulation
  • Crystallization
  • Escherichia coli Proteins*
  • HSP70 Heat-Shock Proteins / chemistry*
  • HSP70 Heat-Shock Proteins / metabolism
  • Humans
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / metabolism
  • Protein Structure, Tertiary*
  • Solutions
  • Substrate Specificity


  • Bacterial Proteins
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Molecular Chaperones
  • Peptide Fragments
  • Solutions
  • dnaK protein, E coli