7L20

Cryo-EM structure of the human 39S mitoribosomal subunit in complex with RRFmt and EF-G2mt.

これはPDB形式変換不可エントリーです。

7L20 の概要

• エントリーDOI: 10.2210/pdb7l20/pdb
• EMDBエントリー: 23121
• 分子名称: 16S rRNA mitochondrial, 39S ribosomal protein L20, mitochondrial, 39S ribosomal protein L21, mitochondrial, ... (59 entities in total)
• 機能のキーワード: cryo-em, mammalian, mito-ribosome, mtefg2, mtrrf, ribosome
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 1906439.05

構造登録者

Agrawal, E.,Koripella, R. (登録日: 2020-12-15, 公開日: 2021-05-12, 最終更新日: 2024-11-20)

主引用文献

Koripella, R.K.,Deep, A.,Agrawal, E.K.,Keshavan, P.,Banavali, N.K.,Agrawal, R.K.
Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.
Nat Commun, 12:3607-3607, 2021

PubMed Abstract: Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF) and a recycling-specific homolog of elongation factor G (EF-G2). These structures clarify an unusual role of a mitochondria-specific segment of RRF, identify the structural distinctions that confer functional specificity to EF-G2, and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling. Furthermore, biochemical and structural analyses reveal that the molecular mechanism of antibiotic fusidic acid resistance for EF-G2 is markedly different from that of mitochondrial elongation factor EF-G1, suggesting that the two human EF-Gs have evolved diversely to negate the effect of a bacterial antibiotic.

PubMed: 34127662
DOI: 10.1038/s41467-021-23726-4

実験手法

ELECTRON MICROSCOPY (3.15 Å)