Fig. 6: Molecular dynamics (MD) simulations of WT and S109Q/T13A yHsp90.
From: Evolution of the conformational dynamics of the molecular chaperone Hsp90
A MD simulations of the full-length yHsp90 suggest that the S109Q/T13A mutations result in conformational changes in the NTD, particularly around the ATP lid, and residues surrounding the ATP binding site. B Dynamic changes in the ATP lid (Tyr47-Ser/Gln109 distance) and C ion-pairs affecting Hsp90 dimerization (Glu11-Lys98 distance). D Introduction of the S109Q/T13A mutation results in an opening of the ATP binding site in simulations of the NTD construct (see Methods). E Conformational dynamics of the NTD (from full length yHsp90 simulations) indicated by the changes in root-mean-square-fluctuation (rmsf). See also Supplementary Figs. 14–16 for further analysis.
