Fig. 3: Lis1 binding to dynein expands dynein’s conformational landscape.
From: Multiple steps of dynein activation by Lis1 visualized by cryo-EM
a–d, Models of dynein bound to Lis1 for the bent (B6) (a) and intermediate (I5) (b) dynein from the same dataset (dynein with Lis1 incubated for 30 min with ATP), and straight with Lis1 bound (S3) (c) and straight with no Lis1 bound (S2) (d) dynein from the same dataset (dynein with Lis1 incubated for 0.5 min with ATP), fit into their corresponding cryo-EM density maps. Each structural element is colored according to the dynein schematic in Fig. 1a. To the right of each fitted model are views of the nucleotide binding pockets for AAA1 and AAA3 and of the stalk conformations. e, Additional cryo-EM maps obtained after heterogeneity analysis of bent (blue box) and intermediate (green box) dynein conformations from the dynein with Lis1 incubated for 0.5 min with ATP dataset after 3D classification show one or two Lis1 bound to dynein. f, Comparison of linker (magenta) in straight linker dynein (S3, yellow) bound to Lis1 with linker (white) in straight linker dynein (S2, white) with no Lis1 bound. The models were aligned on the basis of the position of AAA1. g, Comparison of models built for intermediate state dynein (I6, green) bound to two Lis1 β-propellers (gray) with straight linker dynein (S3, yellow) bound to one Lis1 β-propeller (white). The two Lis1-binding sites are highlighted. The models were aligned on the basis of the position of Lis1 bound to sitering. h, The dynein and Lis1 binding sites from g.
