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. 2021 Sep 6;28(9):713–723. doi: 10.1038/s41594-021-00637-y

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© The Author(s) 2021

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. 3 — a, Comparison of tRNA structures for human pre-(mt)tRNA^Tyr in the mtRNase P complex (red) and yeast tRNA^Phe in complex with the A. thaliana PRORP1 (At-PRORP1) PPR domain (orange) (PDB 6LVR)²⁷. The two tRNA structures are aligned with the acceptor and T arms (pre-tRNA^Tyr: residues 1–7 and 44–65; tRNA^Phe: residues 1–7 and 49–72). In the mtRNase P complex, the pre-tRNA^Tyr adopts a distorted structure compared to a canonical tRNA, resulting in an approximately 17 Å displacement of the anticodon loop (distance between phosphate atoms between anticodon residues 1 and 2, shown as black circles). b, Distance comparison between the D arm and the anticodon arms of pre-tRNA^Tyr in the mtRNase P complex and tRNA^Phe bound to the At-PRORP1 PPR domain. Distances between phosphorous atoms of nucleotide pairs 25–40, 24–41 and 23–42 (canonical tRNA numbering³³) in both tRNAs are shown as dashed lines. The distance between the D and anticodon arms of pre-tRNA^Tyr in the mtRNase P complex (right) is considerably larger than in a tRNA bound to At-PRORP1 (left).