Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Sep 28;14:6071. doi: 10.1038/s41467-023-41845-y

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2023

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/.

PMC Copyright notice

Fig. 3 — a The 3D structure of pre-tRNA^Arg. The color scheme is the same as in Fig. 1c. Close-up views depicting the interactions between pre-tRNA and proteins are shown in panels (b–d) and (f). b Detail view of D arm and anticodon stem recognition by the NTE of TSEN54. Regions (residues 20–75) of TSEN54 NTE are displayed. Key residues that are involved in recognition are shown as sticks. The nucleobases in the A-I base pair (yellow) and the 3′ bugle (green and gray) are shown as sticks. The last bulge nucleotide, A53, forms hydrogen-bonding interaction with the A-I base pair. c Recognition of the acceptor stem by TSEN54. R41 from P-loop of TSEN34 is also indicated. d Electrostatic surface of the TSEN complex, showing charged interface with the pre-tRNA. The positions of the elbow region and TSEN34 Lα are labeled. e Sequence alignment of the N-terminal insertion of selected vertebrate TSEN54 homologs. The secondary structure elements in the human TSEN54 structure are shown. Strictly conserved residues are marked in white with a red background, and well-conserved residues in red. The region that interacts with pre-tRNA is indicated in blue dots, and that with TSEN15 in orange dots. Hs: human; Mm: mouse; Ss: pig; Am: alligator; Xl: frog; Dr: zebrafish. f Interfaces between TSEN2 and pre-tRNA.