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Science 18 April 1997:
Vol. 276. no. 5311, pp. 431 - 435
DOI: 10.1126/science.276.5311.431
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Reports

Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK

Celia J. Harrison, Manajit Hayer-Hartl, Maurizio Di Liberto, F.-Ulrich Hartl, John Kuriyan *

The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha  helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.

C. J. Harrison and J. Kuriyan, Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
M. Hayer-Hartl, M. Di Liberto, F.-U. Hartl, Cellular Biochemistry and Biophysics Program, Howard Hughes Medical Institute, and Memorial Sloan-Kettering Cancer Center, 1275 York Avenue New York, NY 10021, USA. After 15 June 1997, these authors will be at Max-Planck-Institute for Biochemistry, Am Klopferspitz 18A, 82152 Martinsried, Germany.
*   To whom correspondence should be addressed.

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