| Title | Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. |
| Publication Type | Journal Article |
| Year of Publication | 1997 |
| Authors | Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J |
| Journal | Science |
| Volume | 276 |
| Issue | 5311 |
| Pagination | 431-5 |
| Date Published | 1997 Apr 18 |
| ISSN | 0036-8075 |
| Keywords | Adenosine Diphosphate, Adenosine Triphosphatases, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Dimerization, Escherichia coli Proteins, Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Hydrogen Bonding, Models, Molecular, Molecular Chaperones, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary |
| 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. |
| DOI | 10.1126/science.276.5311.431 |
| Alternate Journal | Science |
| PubMed ID | 9103205 |
Related Faculty:
Maurizio DiLiberto, Ph.D.