Fig. 1: Dynamic view of nucleotide-free HtpG.
From: The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding
a Domain organization of HtpG, illustrating the three principal domains: N-terminal domain (NTD), middle domain (MD), and C-terminal domain (CTD). b Schematic of the conformational transitions of HtpG throughout the chaperone cycle, highlighting various states and existing controversies. c Analysis of nucleotide-free HtpG dynamics across different timescales based on its structural context (PDB 2IOQ). The left panel shows methyl groups in HtpG colored according to their S2 values, representing rigidity, while the right panel colors methyl groups by their microsecond to millisecond timescale exchange rates (kex). Dashed boxes emphasize detailed profiles of representative residues crucial to HtpG function, accompanied by zoomed-in structural views. More detailed views of the dynamics of nucleotide-free HtpG are presented in Fig. S1.
