1US7

Complex of Hsp90 and P50

Summary for 1US7

• Entry DOI: 10.2210/pdb1us7/pdb
• Related: 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7
• Descriptor: HEAT SHOCK PROTEIN HSP82, HSP90 CO-CHAPERONE CDC37 (3 entities in total)
• Functional Keywords: chaperone co-chaperone regulation, chaperone, atp-binding, heat shock
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 2
• Total formula weight: 55077.68

Authors

Roe, S.M.,Ali, M.M.U.,Pearl, L.H. (deposition date: 2003-11-20, release date: 2004-01-15, Last modification date: 2023-12-13)

Primary citation

Roe, S.M.,Ali, M.M.U.,Meyer, P.,Vaughan, C.K.,Panaretou, B.,Piper, P.W.,Prodromou, C.,Pearl, L.H.
The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50(Cdc37)
Cell(Cambridge,Mass.), 116:87-, 2004

PubMed Abstract: Recruitment of protein kinase clients to the Hsp90 chaperone involves the cochaperone p50(cdc37) acting as a scaffold, binding protein kinases via its N-terminal domain and Hsp90 via its C-terminal region. p50(cdc37) also has a regulatory activity, arresting Hsp90's ATPase cycle during client-protein loading. We have localized the binding site for p50(cdc37) to the N-terminal nucleotide binding domain of Hsp90 and determined the crystal structure of the Hsp90-p50(cdc37) core complex. Dimeric p50(cdc37) binds to surfaces of the Hsp90 N-domain implicated in ATP-dependent N-terminal dimerization and association with the middle segment of the chaperone. This interaction fixes the lid segment in an open conformation, inserts an arginine side chain into the ATP binding pocket to disable catalysis, and prevents trans-activating interaction of the N domains.

PubMed: 14718169
DOI: 10.1016/S0092-8674(03)01027-4

Experimental method

X-RAY DIFFRACTION (2.3 Å)