1USU

The Structure of the complex between Aha1 and HSP90

Summary for 1USU

• Entry DOI: 10.2210/pdb1usu/pdb
• Related: 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USV
• Descriptor: HEAT SHOCK PROTEIN HSP82, AHA1, GLYCEROL, ... (4 entities in total)
• Functional Keywords: chaperone-complex, chaperone, activator, hsp90
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 2
• Total formula weight: 49697.54

Authors

Meyer, P.,Roe, S.M.,Pearl, L.H. (deposition date: 2003-12-01, release date: 2004-01-29, Last modification date: 2023-12-13)

Primary citation

Meyer, P.,Prodromou, C.,Liao, C.,Hu, B.,Roe, S.M.,Vaughan, C.K.,Vlasic, I.,Panaretou, B.,Piper, P.W.,Pearl, L.H.
Structural Basis for Recruitment of the ATPase Activator Aha1 to the Hsp90 Chaperone Machinery.
Embo J., 23:1402-, 2004

PubMed Abstract: Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts with the central segment of Hsp90. The structural basis for this interaction is revealed by the crystal structure of the N-terminal domain (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the middle segment of Hsp90 (273-530). Structural analysis and mutagenesis show that binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone.

PubMed: 15039704
DOI: 10.1038/SJ.EMBOJ.7600141

Experimental method

X-RAY DIFFRACTION (2.15 Å)