1usv
From Proteopedia
|
THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90
Overview
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.
About this Structure
1USV is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery., Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH, EMBO J. 2004 Mar 24;23(6):1402-10. PMID:15039704
Page seeded by OCA on Wed Nov 21 04:18:39 2007
