Dynamic Aha1 co‐chaperone binding to human Hsp90
2019 | journal article. A publication with affiliation to the University of Göttingen.
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- Authors
- Oroz, Javier; Blair, Laura J.; Zweckstetter, Markus
- Abstract
- Hsp90 is an essential chaperone that requires large allosteric changes to determine its ATPase activity and client binding. The co-chaperone Aha1, which is the major ATPase stimulator in eukaryotes, is important for regulation of Hsp90's allosteric timing. Little is known, however, about the structure of the Hsp90/Aha1 complex. Here, we characterize the solution structure of unmodified human Hsp90/Aha1 complex using NMR spectroscopy. We show that the 214-kDa complex forms by a two-step binding mechanism and adopts multiple conformations in the absence of nucleotide. Aha1 induces structural changes near Hsp90's nucleotide-binding site, providing a basis for its ATPase-enhancing activity. Our data reveal important aspects of this pivotal chaperone/co-chaperone interaction and emphasize the relevance of characterizing dynamic chaperone structures in solution.
- Issue Date
- 2019
- Journal
- Protein Science
- Organization
- Universitätsmedizin Göttingen
- ISBN
- 31299134
- ISSN
- 1469-896X; 0961-8368
- eISSN
- 1469-896X
- Language
- English