Supplementary Figure 5: Features of the Api137-RF1-70S complex.
From: An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome
a, RF1 (orange), deacylated P-site tRNA (green) and Api137 (salmon) in the Api137-RF1-70S complex. The position of RF1 during canonical termination is shown in blue (PDBID 5J30; Pierson, W. E. et al., Cell Rep. 17, 11-18 (2016)). Boxed regions are zoomed in the panels (b) and (c). b, Interaction of the PAT motif of RF1 (orange) with the UAG stop codon of the mRNA (cyan) in the Api137-RF1-70S complex. c, A2602 of the 23S rRNA is in the rotated conformation as observed in previous RF1-70S structures (Korostelev, A. et al., EMBO J. 29, 2577-2585 (2010); Pierson, W. E. et al., Cell Rep. 17, 11-18 (2016); Laurberg, M. et al., Nature 454, 852-857 (2008); Svidritskiy, E. & Korostelev, A. A., Structure 23, 2155-2161 (2015)). Conformation of A2602 (gray) in Api137-RF1-70S complex compared to A2602 (blue) during canonical termination (PDBID 5J30; Pierson, W. E. et al., Cell Rep. 17, 11-18 (2016)) and A2602 (slate) from the pre-attack state (PDBID 1VY4; Polikanov, Y. S., Steitz, T. A. & Innis, C. A., Nat. Struct. Mol. Biol. 21, 787-793 (2014)). Api137 (salmon) and P-site tRNA (green) are shown for reference. d, e, The binding position of Api137 (salmon) relative to the (d) MifM nascent chain (dark green; Sohmen, D. et al., Nat. Commun. 6, 6941 (2015)) or (e) antimicrobial peptide Onc112 (slate; Seefeldt, A. C. et al., Nat. Struct. Mol. Biol. 22, 470-475 (2015)). In (d) and (e) the orientations of the peptides are indicated.
