5OOL
Structure of a native assembly intermediate of the human mitochondrial ribosome with unfolded interfacial rRNA
5OOL の概要
| エントリーDOI | 10.2210/pdb5ool/pdb |
| EMDBエントリー | 3842 |
| 分子名称 | 16S ribosomal RNA, 39S ribosomal protein L14, mitochondrial, 39S ribosomal protein L15, mitochondrial, ... (59 entities in total) |
| 機能のキーワード | ribosome, mitochondria, biogenesis, translation, electron cryomicroscopy |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 56 |
| 化学式量合計 | 1797380.72 |
| 構造登録者 | Brown, A.,Rathore, S.,Kimanius, D.,Aibara, S.,Bai, X.C.,Rorbach, J.,Amunts, A.,Ramakrishnan, V. (登録日: 2017-08-08, 公開日: 2017-09-13, 最終更新日: 2025-12-17) |
| 主引用文献 | Brown, A.,Rathore, S.,Kimanius, D.,Aibara, S.,Bai, X.C.,Rorbach, J.,Amunts, A.,Ramakrishnan, V. Structures of the human mitochondrial ribosome in native states of assembly. Nat. Struct. Mol. Biol., 24:866-869, 2017 Cited by PubMed Abstract: Mammalian mitochondrial ribosomes (mitoribosomes) have less rRNA content and 36 additional proteins compared with the evolutionarily related bacterial ribosome. These differences make the assembly of mitoribosomes more complex than the assembly of bacterial ribosomes, but the molecular details of mitoribosomal biogenesis remain elusive. Here, we report the structures of two late-stage assembly intermediates of the human mitoribosomal large subunit (mt-LSU) isolated from a native pool within a human cell line and solved by cryo-EM to ∼3-Å resolution. Comparison of the structures reveals insights into the timing of rRNA folding and protein incorporation during the final steps of ribosomal maturation and the evolutionary adaptations that are required to preserve biogenesis after the structural diversification of mitoribosomes. Furthermore, the structures redefine the ribosome silencing factor (RsfS) family as multifunctional biogenesis factors and identify two new assembly factors (L0R8F8 and mt-ACP) not previously implicated in mitoribosomal biogenesis. PubMed: 28892042DOI: 10.1038/nsmb.3464 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.06 Å) |
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