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. 2019 Nov 27;10:5397. doi: 10.1038/s41467-019-13408-7

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© The Author(s) 2019

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. 5 — BrfA recruits and stabilizes the open conformation of RF2 on the ribosome. a, b Overview of the interaction of BrfA (blue) with (a) RF2 (RF2_BrfA, orange) from the BrfA-RF2-ns70S and with (b) RF2 (RF2_stop, lime, PDB ID 4V5E) from a canonical termination complex⁴⁸. RF2 domains 1–4 (d1–d4) and relative positions of the decoding center (DC) and peptidyltransferase center (PTC) are indicated. c Comparison of the relative positions of the SPF motif of RF2_stop (lime) and RF2_BrfA (orange) with BrfA (blue), P-site tRNA (green), and truncated non-stop mRNA (TR-mRNA, cyan) shown for reference. d Interaction between Trp307 (W307, equivalent to B. subtilis Trp318 (W318)) of the switch region of Thermus thermophilus RF2_stop (lime) and A1492 of the 16S rRNA (green) during decoding of the UGA stop codon of the mRNA (cyan). W318 in the switch loop of B. subtilis RF2 (RF2_BrfA, orange) observed upon BrfA binding is superimposed and arrowed. e Same view as in d, but showing the conformation of the switch loop of RF2_BrfA (orange) and A1492/A1493 (yellow) when BrfA (blue) is present. f Superimposition of the conformation of α-helix α7 of RF2 from the crystal structure of the closed form of RF2 (RF2_closed; dark blue, PDB ID 1GQE) with RF2_stop (lime) and RF2_BrfA (orange), with BrfA (blue) shown for reference.