8WKP

Structural basis of translation inhibition by a valine tRNA-derived fragment

これはPDB形式変換不可エントリーです。

8WKP の概要

• エントリーDOI: 10.2210/pdb8wkp/pdb
• EMDBエントリー: 37604
• 分子名称: RNA (1328-MER), 30S ribosomal protein S12, 30S ribosomal protein S15, ... (29 entities in total)
• 機能のキーワード: sulfolobus acidocaldarius ribosome, ribosome
• 由来する生物種: Sulfolobus acidocaldarius DSM 639; 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 892487.91

構造登録者

Wang, Y.H.,Zhou, J. (登録日: 2023-09-28, 公開日: 2024-04-10, 最終更新日: 2025-02-05)

主引用文献

Wu, Y.,Ni, M.T.,Wang, Y.H.,Wang, C.,Hou, H.,Zhang, X.,Zhou, J.
Structural basis of translation inhibition by a valine tRNA-derived fragment.
Life Sci Alliance, 7:-, 2024

PubMed Abstract: Translational regulation by non-coding RNAs is a mechanism commonly used by cells to fine-tune gene expression. A fragment derived from an archaeal valine tRNA (Val-tRF) has been previously identified to bind the small subunit of the ribosome and inhibit translation in Here, we present three cryo-electron microscopy structures of Val-tRF bound to the small subunit of ribosomes at resolutions between 4.02 and 4.53 Å. Within these complexes, Val-tRF was observed to bind to conserved RNA-interacting sites, including the ribosomal decoding center. The binding of Val-tRF destabilizes helices h24, h44, and h45 and the anti-Shine-Dalgarno sequence of 16S rRNA. The binding position of this molecule partially overlaps with the translation initiation factor aIF1A and occludes the mRNA P-site codon. Moreover, we found that the binding of Val-tRF is associated with steric hindrance of the H69 base of 23S rRNA in the large ribosome subunit, thereby preventing 70S assembly. Our data exemplify how tRNA-derived fragments bind to ribosomes and provide new insights into the mechanisms underlying translation inhibition by Val-tRFs.

PubMed: 38599770
DOI: 10.26508/lsa.202302488

実験手法

ELECTRON MICROSCOPY (4.62 Å)