Extended Data Fig. 6: Structural and conservation analysis of the Rip1_Eco-ST^WT complex.

a, Cryo-EM density maps of the Rip1_Eco-ST^WT complex, composed of 12 subunits of Rip1_Eco (blue) and 11 subunits of ST^WT (orange). Top-down, side, and bottom views of the complex are shown. b, Ribbon structure of a representative Rip1_Eco dimer from the Rip1_Eco-ST^WT complex, with each monomer shown in a different color. Each monomer consists of residues 38 to 163 and contains a C₄-type zinc ribbon finger domain at the C-terminal end. c, A magnified view of the interaction interface between one Rip1_Eco and multiple subunits of ST^WT. Cyan dashed lines represent hydrogen bonds; purple dashed lines indicate nonbonded contacts between side chains, reflecting close packing or van der Waals interactions (overlap ≥ –0.4 Å). d, Structure of the Rip1_Eco dodecamer, with ribbons colored based on per-residue conservation scores from ConSurf. Variable regions are colored in cyan, while the rest of the structure is colored in grey. The N- and C-termini are also labeled. e, Amino acid sequence of Rip1_Eco colored based on ConSurf conservation scores. Highly conserved residues are shown in magenta, and variable regions are shown in cyan. Residues within the C₄-type zinc-ribbon domain are boxed.