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. 2020 Jun 10;11:2932. doi: 10.1038/s41467-020-16503-2

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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. 5 — a Comparison of mtIF2 binding in mtPIC-2 with the complete initiation complex (PDB ID: 6GAW). Upon association of the mtLSU (blue), required for complete initiation complex, the mtIF2-domain IV moves towards the mtSSU. The conformational change is represented by the difference vectors for each C_α atom of domain IV. For the other domains, the flexibility is represented through ribbon thickness according to B-factor. b Zoom-in panels showing contacts of the mtIF2-specific insert and linker domain with the mtSSU. c Schematic representation of the mtIF2 with the corresponding color-code to the conformational changes.