1AM1
ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE
Summary for 1AM1
| Entry DOI | 10.2210/pdb1am1/pdb |
| Descriptor | HEAT SHOCK PROTEIN 90, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | chaperone, nucleotide binding site |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm: P02829 |
| Total number of polymer chains | 1 |
| Total formula weight | 24504.59 |
| Authors | Pearl, L.H.,Roe, S.M.,Prodromou, C. (deposition date: 1997-06-20, release date: 1998-06-24, Last modification date: 2024-05-22) |
| Primary citation | Prodromou, C.,Roe, S.M.,O'Brien, R.,Ladbury, J.E.,Piper, P.W.,Pearl, L.H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone Cell(Cambridge,Mass.), 90:65-75, 1997 Cited by PubMed Abstract: Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function. PubMed: 9230303DOI: 10.1016/S0092-8674(00)80314-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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