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6NU3

Structural insights into unique features of the human mitochondrial ribosome recycling

これはPDB形式変換不可エントリーです。
6NU3 の概要
エントリーDOI10.2210/pdb6nu3/pdb
EMDBエントリー0515
分子名称16S rRNA, 39S ribosomal protein L14, mitochondrial, 39S ribosomal protein L15, mitochondrial, ... (87 entities in total)
機能のキーワードmitochondrial ribosome recycling factor, mtrrf, 55s, ribosome
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数85
化学式量合計2799251.39
構造登録者
Sharma, M.R.,Koripella, R.K.,Agrawal, R.K. (登録日: 2019-01-30, 公開日: 2019-04-17, 最終更新日: 2024-10-23)
主引用文献Koripella, R.K.,Sharma, M.R.,Risteff, P.,Keshavan, P.,Agrawal, R.K.
Structural insights into unique features of the human mitochondrial ribosome recycling.
Proc.Natl.Acad.Sci.USA, 116:8283-8288, 2019
Cited by
PubMed Abstract: Mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with bacteria, the composition and structure of the human mitoribosome and its translational factors are significantly different from those of their bacterial counterparts. The mammalian mitoribosome recycling factor (RRF) carries a mito-specific N terminus extension (NTE), which is necessary for the function of RRF Here we present a 3.9-Å resolution cryo-electron microscopic (cryo-EM) structure of the human 55S mitoribosome-RRF complex, which reveals α-helix and loop structures for the NTE that makes multiple mito-specific interactions with functionally critical regions of the mitoribosome. These include ribosomal RNA segments that constitute the peptidyl transferase center (PTC) and those that connect PTC with the GTPase-associated center and with mitoribosomal proteins L16 and L27. Our structure reveals the presence of a tRNA in the pe/E position and a rotation of the small mitoribosomal subunit on RRF binding. In addition, we observe an interaction between the pe/E tRNA and a mito-specific protein, mL64. These findings help understand the unique features of mitoribosome recycling.
PubMed: 30962385
DOI: 10.1073/pnas.1815675116
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4.4 Å)
構造検証レポート
Validation report summary of 6nu3
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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