FIGURE

Fig. 5

ID

ZDB-FIG-200728-18

Publication

Mader et al., 2020 - Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90

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Fig. 5

Characterization of the Hsp90 dimer by FRET and SAXS experiments.

a Chase experiments with the closed wild type (WT, left) and R32A (right) Hsp90 dimers in the apo-form and bound to different nucleotides (ATP, AMP-PNP, ATPγS). Chase experiments were initiated by addition of unlabelled Hsp90. b Left: pair distance distributions (P(r)) obtained from the SAXS profiles of apo wild-type (WT) Hsp90 (purple) and bound to different nucleotides (ADP, ATP, AMP-PNP). The P(r) distribution calculated from the X-ray structure of Hsp90 in the closed conformation (PDB ID: 2CG9)⁹ is shown for comparison (in black). Right: pair distance distributions of the R32A variant in different nucleotide states. AMP-PNP favours a compact conformation of wild-type (WT) Hsp90, whereas the R32A variant shows no major conformational rearrangements.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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