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Structural Insights into the Slicer Catalytic Site of AfPiwi and PfAgo

This supplementary figure illustrates the putative slicer catalytic site of AfPiwi and PfAgo11 by superimposing their RNase H domains. The analysis reveals the position of catalytic aspartates (Asp) in PfAgo, which are essential for function, along with Glu264 in AfPiwi that contributes to the DDE triad necessary for catalytic activity. The distance between the catalytic Asp residues and the scissile phosphate is detailed, emphasizing the structural alignment of key residues involved in RNA slicing. The guide strand is excluded for clarity.

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Structural Insights into the Slicer Catalytic Site of AfPiwi and PfAgo

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  1. AfPiwi Leu427 scissile phosphate target strand Glu264 catalytic aspartates PfAgo Supplementary Figure 3. Details of the putative slicer catalytic site. The RNase H domains of AfPiwi (orange) and PfAgo11 (violet) are superimposed, and the putative magnesium dependent RNase H-like catalytic Asps present in PfAgo are displayed. An invariant Glu (Glu 264 in AfPiwi) which completes the DDE triad is displayed in both proteins. The catalytic Asps approach the scissile phosphate within 10-11 Å. Residue numbers are for AfPiwi. The guide strand is omitted for clarity.

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