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DOI | 10.2210/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 | |
| 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: 30962385DOI: 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) |
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