Extended Data Fig. 4: ΦKZ014 structure and interaction sites.
From: Phage proteins target and co-opt host ribosomes immediately upon infection
a, The predicted structure of ΦKZ014 determined with AlphaFold2/ColabFold suggested an N-terminal helix, a β-fold domain, a central domain, a disordered region and a C-terminal helix-loop-helix (HLH) domain. b, Electrostatic surface potential of ΦKZ014 displayed in the orientation from the 5S rRNA interface side. The position of the 5S rRNA clamp is labelled. c, ΦKZ014 interacts with the 23S rRNA backbone at positions U908 and A909 via two sequential His178 and His179 residues. This is near 5S rRNA A94-G98. Lys152 points in the direction of 5S rRNA backbone. d, Key interacting residues (R10, K15, W18, R23, K152, R262, K263) are conserved in ΦKZ014 homologs.
