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. 2020 Feb 26;11:1077. doi: 10.1038/s41467-020-14943-4

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Three major Ric-8A:Gα contact surfaces and phosphorylation sites are highlighted in the green, yellow, pink, and blue overlays (panel a) and enlarged in panels b–e. Axes adjacent to each panel label indicate the rotation applied to the overall schematic to generate the panel view. b Interaction between Gα β-sheet and the Ric-8A C-terminal ARM/HEAT repeat helix rαbA9 and reverse turn r451–r457 (rRT) from the crystal structure. Polypeptide backbones are rendered as tubes, with diameter proportional to B-factor at Cα. Carbon atoms of Ric-8A and Gαi1 are rendered in deep brown, and green, respectively, and oxygen and nitrogen atoms are, respectively, colored red and blue. c Acidic Ric-8A peptide with phosphorylated residues rpS335 and rpT440 bound to the positively charged surface formed by the 8th and 9th Ric-8A ARM/HEAT repeats from the crystal structure. d Interaction of rα11 with gα3 and Switch II from cryo-EM. Putative hydrogen bonds (donor–acceptor contact < 3.5 Å) are depicted with orange dashed lines. e Contacts between gα5 and residues in successive ARM/HEAT repeats of Ric-8A, from the crystal structure.