2CG9
Crystal structure of an Hsp90-Sba1 closed chaperone complex
Summary for 2CG9
Entry DOI | 10.2210/pdb2cg9/pdb |
Related | 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USU 1USV 2AKP 2BRC 2BRE 2CGE |
Descriptor | ATP-DEPENDENT MOLECULAR CHAPERONE HSP82, CO-CHAPERONE PROTEIN SBA1, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
Functional Keywords | chaperone, chaperone complex, hsp90, heat shock protein, co-chaperone, atp-binding, heat shock, nucleotide-binding, acetylation |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
Total number of polymer chains | 4 |
Total formula weight | 188725.33 |
Authors | Ali, M.M.U.,Roe, S.M.,Prodromou, C.,Pearl, L.H. (deposition date: 2006-03-01, release date: 2006-04-12, Last modification date: 2023-12-13) |
Primary citation | Ali, M.M.U.,Roe, S.M.,Vaughan, C.,Meyer, P.,Panaretou, B.,Piper, P.W.,Prodromou, C.,Pearl, L.H. Crystal Structure of an Hsp90-Nucleotide-P23/Sba1 Closed Chaperone Complex Nature, 440:1013-, 2006 Cited by PubMed Abstract: Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for the assembly and regulation of many eukaryotic signalling systems and is an emerging target for rational chemotherapy of many cancers. Although the structures of isolated domains of Hsp90 have been determined, the arrangement and ATP-dependent dynamics of these in the full Hsp90 dimer have been elusive and contentious. Here we present the crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1. The structure reveals the complex architecture of the 'closed' state of the Hsp90 chaperone, the extensive interactions between domains and between protein chains, the detailed conformational changes in the amino-terminal domain that accompany ATP binding, and the structural basis for stabilization of the closed state by p23/Sba1. Contrary to expectations, the closed Hsp90 would not enclose its client proteins but provides a bipartite binding surface whose formation and disruption are coupled to the chaperone ATPase cycle. PubMed: 16625188DOI: 10.1038/NATURE04716 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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