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

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a Three distinct interaction sites between Ebp1 and the consensus sequences cs1 and cs2 mediate ES27L binding. The atomic models for Ebp1 and ES27L are superposed to the cryo-EM density after 3-body multibody refinement. Density was faded out toward the Ebp1–ribosome contact, which is better resolved in the reconstruction from 2-body multibody refinement. View is the same as in Fig. 1a left panel and as indicated by the small representation in the corner. b Consensus sequences (cs) of ES27L involved in Ebp1 binding. Conserved mismatches within cs1 are highlighted. c, d Structural details of ES27L interaction of the GA mismatch at cs1 with the Ebp1 P-loop structure (δ⁺: partial positive charge) following helix α2 (c), and of the GU wobble with Ebp1 helix α1 (d). Putative protein–RNA interactions are indicated by arrows. e Interactions at cs2 with the lysine-rich motif (KRM) within the Ebp1-specific C-terminal helix α C. The putative GG cross-strand purine stack is indicated by parallel lines.