Fig. 1: Time-resolved cryo-EM captures Lis1’s effect on dynein’s conformational landscape during ATP hydrolysis.
From: Multiple steps of dynein activation by Lis1 visualized by cryo-EM
a, Schematic of dynein domain organization. Lis1 binding at different sites on dynein (sitering and sitestalk) is shown in different dynein conformations43. MTBD, microtubule-binding domain. b, The architecture of a nucleotide-binding pocket and Stalk–MTBD communication. c, Schematic of the experimental setup. d–f, The three major groups of conformations identified in the datasets are shown on locally refined cryo-EM volumes, filtered to 6 Å: straight linker (d), intermediate linker (e), and bent linker (f). The linker region is highlighted in magenta. The extent of ring opening is shown to the left of each panel. g, Different conformations were identified in each dataset in the absence (open circle) or presence of Lis1 (black circle) at two different time points (0.5 min, white background; 30 min, gray background). h, Relative abundance of particles belonging to different states obtained from particle distributions in cryo-EM datasets in the absence (open circle) or presence of Lis1 (black circle) at two different time points (0.5 min, white background; 30 min, gray background).
