7A5K

Structure of the human mitoribosome in the post translocation state bound to mtEF-G1

これはPDB形式変換不可エントリーです。

7A5K の概要

• エントリーDOI: 10.2210/pdb7a5k/pdb
• EMDBエントリー: 11646
• 分子名称: Elongation factor G, mitochondrial, 39S ribosomal protein L11, mitochondrial, 39S ribosomal protein L13, mitochondrial, ... (95 entities in total)
• 機能のキーワード: mitochondrial ribosome, ribosome stalling, cryo-em, ribosome
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 93
• 化学式量合計: 3627409.94

構造登録者

Desai, N.,Yang, H.,Chandrasekaran, V.,Kazi, R.,Minczuk, M.,Ramakrishnan, V. (登録日: 2020-08-21, 公開日: 2020-12-23, 最終更新日: 2025-12-17)

主引用文献

Desai, N.,Yang, H.,Chandrasekaran, V.,Kazi, R.,Minczuk, M.,Ramakrishnan, V.
Elongational stalling activates mitoribosome-associated quality control.
Science, 370:1105-1110, 2020

PubMed Abstract: The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase.

PubMed: 33243891
DOI: 10.1126/science.abc7782

実験手法

ELECTRON MICROSCOPY (3.7 Å)