1DKG
CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK
Summary for 1DKG
| Entry DOI | 10.2210/pdb1dkg/pdb |
| Descriptor | NUCLEOTIDE EXCHANGE FACTOR GRPE, MOLECULAR CHAPERONE DNAK (3 entities in total) |
| Functional Keywords | hsp70, grpe, molecular chaperone, nucleotide exchange factor, coiled-coil, complex (hsp24-hsp70), complex (hsp24-hsp70) complex, complex (hsp24/hsp70) |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm (Probable): P09372 Cytoplasm: P04475 |
| Total number of polymer chains | 3 |
| Total formula weight | 85337.81 |
| Authors | Harrison, C.J.,Kuriyan, J. (deposition date: 1997-02-13, release date: 1997-08-20, Last modification date: 2024-02-07) |
| Primary citation | Harrison, C.J.,Hayer-Hartl, M.,Di Liberto, M.,Hartl, F.,Kuriyan, J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science, 276:431-435, 1997 Cited by PubMed 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. PubMed: 9103205DOI: 10.1126/science.276.5311.431 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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