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. 2016 Dec 20;7:13521. doi: 10.1038/ncomms13521

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Copyright © 2016, The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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(a) Superposition of the atomic models for eukaryotic A/T tRNA (grey) during decoding and Dom34 on the nonstop-stalled ribosome. The N-terminal domain of Dom34 is coloured hot pink, domain M yellow and domain C green. Both models superpose to a large extent, except for the β-loop of Dom34. (b) Alignment of Dom34/Hbs1 and the archael aPelota/aEF1a complex on the G proteins. The N domains of Dom34 and aPelota are shifted by 6 Å against each other. (c) Structures of Dom34 generally overlap well during nonstop and no-go recognition; however, in particular, domain C shows significant conformational changes.