Fig. 2: The ATP-binding pocket and interactions between helicase domain and C terminus of Loqs-PD.

a, Interactions between the ATP-binding site and RIIIDai from molecule B in the initial binding state. b, Details of the ATP-binding site in the early-translocation state. c, Overview of the Loqs-PD binding sites in the helicase domain of Dcr-2. Loqs-PD is shown as a transparent cryo-EM map. d, Surface presentation of the Loqs-PD binding region in the helicase domain. Loqs-PD is shown as a stick model. The surface is coloured by electrostatic potential. e–g, Details of the interactions of Dcr-2 with Ile359 (e), Phe354 and Phe356 (f), and Tyr347 (g) regions of C terminus of Loqs-PD. h, SDS–PAGE gels of the pull-down result for Dcr-2 with the WT and three variants of His-tagged Loqs-PD. Gel source data are provided in Supplementary Fig. 1. i, Quantification of the pull-down data in h. Data are mean ± s.d. n = 3 biologically independent experiments. Statistical analysis was performed using two-sided paired t-tests; **P < 0.01. The exact P values for WT versus Y347A, F356D and I359D are 0.0037, 0.0063 and 0.0091, respectively.