Structure of a new crystal form of human Hsp70 ATPase domain.

  title={Structure of a new crystal form of human Hsp70 ATPase domain.},
  author={J. Osipiuk and M. Walsh and B. Freeman and R. Morimoto and A. Joachimiak},
  journal={Acta crystallographica. Section D, Biological crystallography},
  volume={55 Pt 5},
  • J. Osipiuk, M. Walsh, +2 authors A. Joachimiak
  • Published 1999
  • Medicine, Chemistry
  • Acta crystallographica. Section D, Biological crystallography
  • Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 A shift of one of the subdomains of the protein. This conformational change… CONTINUE READING
    46 Citations

    Figures, Tables, and Topics from this paper.

    Allostery in the Hsp70 chaperone proteins.
    • 126
    Dissection of the ATP-binding Domain of the Chaperone hsc70 for Interaction with the Cofactor Hap46*
    • 14
    • PDF
    Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state.
    • 15
    • Highly Influenced
    • PDF
    The carboxyl-terminal lobe of Hsc70 ATPase domain is sufficient for binding to BAG1.
    • 38
    The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.
    • Y. Zhang, E. Zuiderweg
    • Chemistry, Medicine
    • Proceedings of the National Academy of Sciences of the United States of America
    • 2004
    • 78
    • PDF
    Conformational dynamics of full-length inducible human Hsp70 derived from microsecond molecular dynamics simulations in explicit solvent
    • 11
    • PDF


    Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • 932
    • Highly Influential
    Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
    • 1,149
    The Hsp70 and Hsp60 Chaperone Machines
    • 2,672
    • Highly Influential
    • PDF
    AMoRe: an automated package for molecular replacement
    • 4,623
    • Highly Influential
    • PDF
    • Structure
    • 1997
    Acta Cryst
    • A32, 922±923.
    • 1978
    Acta Cryst
    • A50, 157±163.
    • 1994