1A4H

STRUCTURE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE IN COMPLEX WITH GELDANAMYCIN

Summary for 1A4H

• Entry DOI: 10.2210/pdb1a4h/pdb
• Descriptor: HEAT SHOCK PROTEIN 90, GELDANAMYCIN (3 entities in total)
• Functional Keywords: chaperone, atp-binding, heat shock
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P02829
• Total number of polymer chains: 1
• Total formula weight: 26695.43

Authors

Prodromou, C.,Roe, S.M.,Pearl, L.H. (deposition date: 1998-01-29, release date: 1998-08-05, 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

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: 9230303
DOI: 10.1016/S0092-8674(00)80314-1

Experimental method

X-RAY DIFFRACTION (2.5 Å)