7ODS

State B of the human mitoribosomal large subunit assembly intermediate

これはPDB形式変換不可エントリーです。

7ODS の概要

• エントリーDOI: 10.2210/pdb7ods/pdb
• EMDBエントリー: 12846
• 分子名称: Mitochondrial assembly of ribosomal large subunit protein 1, 39S ribosomal protein L35, mitochondrial, 39S ribosomal protein L36, mitochondrial, ... (65 entities in total)
• 機能のキーワード: mitoribosome, assembly intermediate, large subunit, lsu, mt-lsu, ribosome
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 1917679.18

構造登録者

Lenarcic, T.,Jaskolowski, M.,Leibundgut, M.,Scaiola, A.,Schoenhut, T.,Saurer, M.,Lee, R.G.,Rackham, O.,Filipovska, A.,Ban, N. (登録日: 2021-04-30, 公開日: 2021-06-23, 最終更新日: 2023-11-15)

主引用文献

Lenarcic, T.,Jaskolowski, M.,Leibundgut, M.,Scaiola, A.,Schonhut, T.,Saurer, M.,Lee, R.G.,Rackham, O.,Filipovska, A.,Ban, N.
Stepwise maturation of the peptidyl transferase region of human mitoribosomes.
Nat Commun, 12:3671-3671, 2021

PubMed Abstract: Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral bacterial ribosomes and feature dramatically reduced ribosomal RNAs. The structural basis of the mammalian mitochondrial ribosome assembly is currently not well understood. Here we present eight distinct assembly intermediates of the human large mitoribosomal subunit involving seven assembly factors. We discover that the NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by the MRM2 methyltransferase and quality control interactions with the conserved mitochondrial GTPase MTG2 that contacts the sarcin-ricin loop and the immature active site. The successive action of these factors leads to the formation of the peptidyl transferase active site of the mitoribosome and the folding of the surrounding rRNA regions responsible for interactions with tRNAs and the small ribosomal subunit.

PubMed: 34135320
DOI: 10.1038/s41467-021-23811-8

実験手法

ELECTRON MICROSCOPY (3.1 Å)