7QI5

Human mitochondrial ribosome in complex with mRNA, A/A-, P/P- and E/E-tRNAs at 2.63 A resolution

これはPDB形式変換不可エントリーです。

7QI5 の概要

• エントリーDOI: 10.2210/pdb7qi5/pdb
• EMDBエントリー: 13981
• 分子名称: 12S mitochondrial rRNA, 28S ribosomal protein S12, mitochondrial, VALINE, ... (101 entities in total)
• 機能のキーワード: ribosome, mitochondrial translation, trna, mrna, 2fe-2s clusters, polyamines, rrna modifications, post-translation modifications, cryo em
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 94
• 化学式量合計: 3136519.25

構造登録者

Singh, V.,Itoh, Y.,Amunts, A. (登録日: 2021-12-14, 公開日: 2023-07-05, 最終更新日: 2024-07-31)

主引用文献

Singh, V.,Itoh, Y.,Del'Olio, S.,Hassan, A.,Naschberger, A.,Flygaard, R.K.,Nobe, Y.,Izumikawa, K.,Aibara, S.,Andrell, J.,Whitford, P.C.,Barrientos, A.,Taoka, M.,Amunts, A.
Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk.
Nat Commun, 15:4272-4272, 2024

PubMed Abstract: The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together with validated mitoribosomal RNA (rRNA) modifications, including aminoacylated CP-tRNA. The structure shows how mitoribosomal proteins stabilise binding of mRNA and tRNA helping to align it in the decoding center, whereas the GDP-bound mS29 stabilizes intersubunit communication. Comparison between different states, with respect to tRNA position, allowed us to characterize a non-canonical L1 stalk, and molecular dynamics simulations revealed how it facilitates tRNA transitions in a way that does not require interactions with rRNA. We also report functionally important polyamines that are depleted when cells are subjected to an antibiotic treatment. The structural, biochemical, and computational data illuminate the principal functional components of the translation mechanism in mitochondria and provide a description of the structure and function of the human mitoribosome.

PubMed: 38769321
DOI: 10.1038/s41467-024-48163-x

実験手法

ELECTRON MICROSCOPY (2.63 Å)