Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Nature. 1990 Aug 16;346(6285):623-8. doi: 10.1038/346623a0.


The three-dimensional structure of the amino-terminal 44K ATPase fragment of the 70K bovine heat-shock cognate protein has been solved to a resolution of 2.2 A. The ATPase fragment has two structural lobes with a deep cleft between them; ATP binds at the base of the cleft. Surprisingly, the nucleotide-binding 'core' of the ATPase fragment has a tertiary structure similar to that of hexokinase, although the remainder of the structures of the two proteins are completely dissimilar, suggesting that both the phosphotransferase mechanism and the substrate-induced conformational change intrinsic to the hexokinases may be used by the 70K heat shock-related proteins.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases*
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle
  • Chemical Phenomena
  • Chemistry, Physical
  • Computer Simulation
  • Crystallization
  • Heat-Shock Proteins*
  • Hexokinase
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Molecular Weight
  • Osmolar Concentration
  • Peptide Fragments*
  • Protein Conformation
  • X-Ray Diffraction


  • Heat-Shock Proteins
  • Macromolecular Substances
  • Peptide Fragments
  • Adenosine Triphosphate
  • Hexokinase
  • Adenosine Triphosphatases

Associated data