Extended Data Fig. 6: The conformational change of the helicase domain induced by dsRNA binding.

a, Superposition of the apo state (grey) and the initial binding state (coloured), aligned by RIIIDs. b, The RMSD values of residues in (a) demonstrate the variation of the two state. The helicase domain is coloured as in Fig. 1a, and the cap-core region is coloured in grey. c, Superposition of the apo state (grey) and the initial binding state (coloured), aligned by the Hel1 domain. The DUF283-cap-core region is shown as EM density in the apo (grey) and initial binding (sky-blue) states, respectively. d, The BS3 cross-linking residues in the apo state (left panel) and the initial binding state (right panel) of the helicase domain. The cross-linked residues are linked by blue line (upper panel) and red dashes (lower panel). e, Summary of distances between BS3 cross-linking residues in the apo state and the initial binding state. The cross-linking sites specific in the apo state are marked in the orange square. The cross-linking sites specific in the initial binding state are marked in the green square. f, The C-terminal region of Loqs-PD is shown in stick model fitted in the EM density in transparency. g, The EDC cross-linking residues between the helicase domain and C-terminal region of Loqs-PD. h–i, Inter-domain contacts of DUF283 with the Hel1 domain (h) and the Hel2i domain (i) in the initial binding state.