1HK7

Middle Domain of HSP90

Summary for 1HK7

• Entry DOI: 10.2210/pdb1hk7/pdb
• Related: 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1US7 1USU 1USV
• Descriptor: HEAT SHOCK PROTEIN HSP82, CADMIUM ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: heat shock protein, atpase, chaperone
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 68435.66

Authors

Meyer, P.,Prodromou, C.,Roe, S.M.,Pearl, L.H. (deposition date: 2003-03-06, release date: 2004-01-29, Last modification date: 2024-05-08)

Primary citation

Meyer, P.,Prodromou, C.,Hu, B.,Vaughan, C.,Roe, S.M.,Panaretou, B.,Piper, P.W.,Pearl, L.H.
Structural and Functional Analysis of the Middle Segment of Hsp90. Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions
Mol.Cell, 11:647-, 2003

PubMed Abstract: Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysis of ATP, which drives a molecular clamp via transient dimerization of the N-terminal domains. The crystal structure of the middle segment of yeast Hsp90 reveals considerable evolutionary divergence from the equivalent regions of other GHKL protein family members such as MutL and GyrB, including an additional domain of new fold. Using the known structure of the N-terminal nucleotide binding domain, a model for the Hsp90 dimer has been constructed. From this structure, residues implicated in the ATPase-coupled conformational cycle and in interactions with client proteins and the activating cochaperone Aha1 have been identified, and their roles functionally characterized in vitro and in vivo.

PubMed: 12667448
DOI: 10.1016/S1097-2765(03)00065-0

Experimental method

X-RAY DIFFRACTION (2.5 Å)