Fig. 4: Structure of phosphomimetic SLFN11^S753D in an ATP-bound state.

a NanoDSF of SLFN11^S753D without or in the presence of different nucleotides. Data are represented as mean values +/− SD from three independent experiments. One representative replicate is shown. Detailed view of the nucleotide-binding region in the helicase domain of SLFN11^S753D. Walker motifs and Q-motif are highlighted in cyan and hot pink, respectively. ATP is colored in black and the magnesium ion is colored in green. b NanoDSF of SLFN11^wt without or in the presence of different nucleotides. Data are represented as mean values +/− SD from three independent experiments. One representative replicate is shown. Detailed view of the nucleotide-binding region in the helicase domain of SLFN11^wt. Walker motifs and Q-motif are highlighted in cyan and hot pink, respectively. c Domain architecture of SLFN11 with indicated key functional features (top). The phosphorylation sites are highlighted in purple. Ribbon representation of the ATP-bound structure of SLFN11^S753D with highlighted structural features (bottom). The unresolved region from residue 747 to 771 is indicated by a dotted line. The approximate position of mutation S753D and the positions of S219 and T230 are indicated in purple. The inset shows the cryo-EM density map around ATP bound to the helicase domain of SLFN11^S753D (surface cutoff: 2 Å). The ATP-bound magnesium ion is colored in green. d Mass distribution of SLFN11^S753D in the presence of 80 mM NaCl observed by mass photometry. e Mass photometry analysis of SLFN11^wt in the presence of 80 mM NaCl showing a monomer-dimer mix. Source data for a and b are provided as a Source Data file.