Journal
STRUCTURE
Volume 13, Issue 4, Pages 579-590Publisher
CELL PRESS
DOI: 10.1016/j.str.2004.12.018
Keywords
-
Funding
- NCI NIH HHS [P30 CA016086] Funding Source: Medline
- NIDDK NIH HHS [DK46249] Funding Source: Medline
- NIGMS NIH HHS [GM059791] Funding Source: Medline
Ask authors/readers for more resources
Hsp90 is an abundant molecular chaperone involved in many biological systems. We report here the crystal structures of the unliganded and ADP bound fragments containing the N-terminal and middle domains of HtpG, an E. coli Hsp90. These domains are not connected through a flexible linker, as often portrayed in models, but are intimately associated with one another. The individual HtpG domains have similar folding to those of DNA gyrase B but assemble differently, suggesting somewhat different mechanisms for the ATPase superfamily. ADP binds to a subpocket of a large site that is jointly formed by the N-terminal and middle domains and induces conformational changes of the N-terminal domain. We speculate that this large pocket serves as a putative site for binding of client proteins/cochaperones. Modeling shows that ATP is not exposed to the molecular surface, thus implying that ATP activation of hsp90 chaperone activities is accomplished via conformational changes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available