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

Harrison, Celia J., Hayer-Hartl, Manajit, Liberto, Maurizio Di, Hartl, F.-Ulrich, Kuriyan, John·1997·Science

Abstract

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 α helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.

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Metadata

Authors
Harrison, C. J., Hayer-Hartl, M., Liberto, M. D., Hartl, F.-U., & Kuriyan, J.
Venue
Science
Published
1997-04-18
Volume
276
Issue
5311
Pages
431-435
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2107334607
Cited by
497
References
0
FWCI
6.75
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK. https://app.cochat.ai/papers/10.1126/science.276.5311.431
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Harrison, C. J., Hayer-Hartl, M., Liberto, M. D., Hartl, F.-U., & Kuriyan, J. (1997). Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK. Science. https://doi.org/10.1126/science.276.5311.431

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