Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK Journal Article

  


Authors: Harrison, C. J.; Hayer-Hartl, M.; Di Liberto, M.; Hartl, F. U.; Kuriyan, J.
Article Title: Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
Abstract: The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coil 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.
Keywords: controlled study; unclassified drug; nonhuman; protein conformation; protein domain; mammalia; adenosine diphosphate; bacterial proteins; amino acid sequence; molecular sequence data; escherichia coli; crystal structure; hydrogen bonding; models, molecular; dimerization; crystallography, x-ray; binding sites; heat shock protein 70; conformational transition; protein folding; adenosine triphosphatase; adenosine triphosphatases; protein structure, secondary; hsp70 heat-shock proteins; escherichia coli proteins; molecular chaperones; alpha helix; heat-shock proteins; nucleotide exchange factor; escherichia; nucleotide binding protein; priority journal; article; protein dnak
Journal Title: Science
Volume: 276
Issue: 5311
ISSN: 0036-8075
Publisher: American Association for the Advancement of Science  
Date Published: 1997-04-18
Start Page: 431
End Page: 435
Language: English
DOI: 10.1126/science.276.5311.431
PUBMED: 9103205
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030936995&doi=10.1126%2fscience.276.5311.431&partnerID=40&md5=01f3bf629fa6411522f9fcef9d98ef57
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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MSK Authors
  1. Maurizio Diliberto
    6 Diliberto
  2. F. Ulrich Hartl
    75 Hartl
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