6ZM6

Human mitochondrial ribosome in complex with mRNA, A/A tRNA and P/P tRNA

これはPDB形式変換不可エントリーです。

6ZM6 の概要

• エントリーDOI: 10.2210/pdb6zm6/pdb
• EMDBエントリー: 11279
• 分子名称: 16S mitochondrial rRNA, 39S ribosomal protein L14, mitochondrial, 39S ribosomal protein L15, mitochondrial, ... (94 entities in total)
• 機能のキーワード: mitochondrion, translation, closed nascent-polypeptide tunnel, ribosome
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 92
• 化学式量合計: 3069299.32

構造登録者

Itoh, Y.,Andrell, J.,Amunts, A. (登録日: 2020-07-01, 公開日: 2021-01-13, 最終更新日: 2023-11-15)

主引用文献

Itoh, Y.,Andrell, J.,Choi, A.,Richter, U.,Maiti, P.,Best, R.B.,Barrientos, A.,Battersby, B.J.,Amunts, A.
Mechanism of membrane-tethered mitochondrial protein synthesis.
Science, 371:846-849, 2021

PubMed Abstract: Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo-electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1-like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery.

PubMed: 33602856
DOI: 10.1126/science.abe0763

実験手法

ELECTRON MICROSCOPY (2.59 Å)