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. 2020 Feb 7;11:776. doi: 10.1038/s41467-020-14603-7

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© The Author(s) 2020

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Fig. 3 — a The insert domain of Ebp1 (blue) binds to the general docking site, including ribosomal proteins uL23 (yellow) and uL29 (orange). Three lysine residues within the MetAP-core fold triangulate 5.8S rRNA helix H24 (green). View is rotated in plane by 180° in respect to Fig. 1c bottom and as indicated by the small representation in the corner. b Bacterial Trigger factor³⁰ (PDB ID: 1W2B) exploits the same binding mode to uL23. c The SRP GTPase SRP54 is incompatible with Ebp1/MetAP binding. The NG domain binds to uL29^{32, 34} (PDB ID: 3JAJ) and does not interfer with the insert domain, while signal-recognizing SRP54M (dark green) competes for uL23 binding (view rotated vertically by 90° to panel (a)). d The Sec61 translocon displaces SRP54 and reaches deep into the tunnel exit up to 28S rRNA H50^{35, 36} (PDB ID: 3J7Q).