Extended Data Fig. 7: AlphaFold3 modelling and mutational analysis of the Rip1Eco-STWT complex.
From: A pore-forming antiphage defence is activated by oligomeric phage proteins
a, AlphaFold3 predicted complex of the 12-mer Rip1EcoΔ1-7aa and 11-mer STWT, colored by predicted Local Distance Difference Test (pLDDT) scores. Only the oligomerization domain of ST is shown to highlight its resemblance to the solved cryo-EM structure in Fig. 2g. b, The Predicted Aligned Error (PAE) plot of the complex shown in (a). Lower PAE values (dark green) indicate high-confidence regions, while higher values (light green) indicate flexibility (lower certainty). Expected positional error ranges from 0 – 30 Å. c, Helical wheel diagram of residues 8 to 30 of Rip1Eco showing the amphipathic nature of the N-terminal α-helix. Nonpolar residues are colored yellow. d, Cryo-EM reconstruction from Fig. 2g, labeled with mutations present in escape mutants of phages T4 and T6. Black arrows represent mutations.
