Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Academic Article uri icon

Overview

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

publication date

  • April 18, 1997

Research

keywords

  • Adenosine Triphosphatases
  • Bacterial Proteins
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Protein Conformation

Identity

Scopus Document Identifier

  • 0030936995

Digital Object Identifier (DOI)

  • 10.1126/science.276.5311.431

PubMed ID

  • 9103205

Additional Document Info

volume

  • 276

issue

  • 5311