Fig. 6: Comparison of the conformational rearrangements in the Hsp90 variants.
From: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
a The nucleotide-induced closure of the FRET pair labelled dimer was monitored in the acceptor channel after addition of the different nucleotides. b ATPγS induced closing kinetics of mono-methylated Hsp90 (K594metK) and WT yeast Hsp90. c Closing kinetics of three independent measurements. Data were fitted using a bi-exponential fit (see methods Eq. 1). The error bars for the turnover rates represent s.d. (n = 3). Statistical significance was assessed using a two-sample t-test and a level of significance of 0.05 (*), 0.01 (**), and 0.001 (***). d The disruption of a preformed FRET complex was followed after adding an excess of unlabelled protein. Left panel shows the kinetics for the WT and the middle and right panel for the K594I and K594E mutants. e Sedimentation profiles of the labelled WT, K594I, and K594E mutants in the absence and presence of the nucleotides ATPγS and AMP-PNP. Source data are provided as a Source Data file.
