The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis

A small molecule that preferentially binds the closed conformation of Hsp90

(2011) Leslie D. Alexander et al.   BIOORGANIC & MEDICINAL CHEMISTRY LETTERS

Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex

(2011) Daniel R. Southworth et al.   MOLECULAR CELL

Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular Chaperone

(2011) Timothy O. Street et al.   MOLECULAR CELL

Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity

(2010) Yuko Motojima-Miyazaki et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Mechanistic Studies of Sansalvamide A-Amide: An Allosteric Modulator of Hsp90

(2010) Robert C. Vasko et al.   ACS Medicinal Chemistry Letters

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

(2009) Moritz Mickler et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

(2009) Martin Hessling et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Intra- and Intermonomer Interactions Are Required to Synergistically Facilitate ATP Hydrolysis in Hsp90

(2008) Christian N. Cunningham et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle

(2008) Daniel R. Southworth et al.   MOLECULAR CELL

Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90

(2008) Kristin A. Krukenberg et al.   STRUCTURE