Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK
Copyright policy )Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK
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.
- MTA Biological Research Centre Hungary
- Memorial Sloan Kettering Cancer Center United States
- Institute of Biochemistry Hungary
- Howard Hughes Medical Institute United States
- Rockefeller University United States
Adenosine Triphosphatases, Models, Molecular, Binding Sites, Protein Conformation, Escherichia coli Proteins, Molecular Sequence Data, Hydrogen Bonding, Crystallography, X-Ray, Protein Structure, Secondary, Adenosine Diphosphate, Bacterial Proteins, HSP70 Heat-Shock Proteins, Amino Acid Sequence, Dimerization, Heat-Shock Proteins, Molecular Chaperones
Adenosine Triphosphatases, Models, Molecular, Binding Sites, Protein Conformation, Escherichia coli Proteins, Molecular Sequence Data, Hydrogen Bonding, Crystallography, X-Ray, Protein Structure, Secondary, Adenosine Diphosphate, Bacterial Proteins, HSP70 Heat-Shock Proteins, Amino Acid Sequence, Dimerization, Heat-Shock Proteins, Molecular Chaperones
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