8PV3
Chaetomium thermophilum pre-60S State 9 - pre-5S rotation - immature H68/H69 - composite structure
これはPDB形式変換不可エントリーです。
8PV3 の概要
エントリーDOI | 10.2210/pdb8pv3/pdb |
EMDBエントリー | 17916 17917 17918 17952 |
分子名称 | 26S rRNA, Ribosome biogenesis protein NSA2 homolog, Putative GTP binding protein, ... (62 entities in total) |
機能のキーワード | biogenesis, pre-60s, 5s rnp, ribosome |
由来する生物種 | Thermochaetoides thermophila DSM 1495 詳細 |
タンパク質・核酸の鎖数 | 59 |
化学式量合計 | 3064129.43 |
構造登録者 | Thoms, M.,Cheng, J.,Denk, T.,Berninghausen, O.,Beckmann, R. (登録日: 2023-07-17, 公開日: 2023-11-15, 最終更新日: 2023-12-20) |
主引用文献 | Thoms, M.,Lau, B.,Cheng, J.,Fromm, L.,Denk, T.,Kellner, N.,Flemming, D.,Fischer, P.,Falquet, L.,Berninghausen, O.,Beckmann, R.,Hurt, E. Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation. Embo Rep., 24:e57984-e57984, 2023 Cited by PubMed Abstract: The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from Chaetomium thermophilum, which consists of two sub-modules, the sphere-like Rix1-Ipi3-Ipi1 and the butterfly-like Las1-Grc3 complex, connected by a flexible linker. The Rix1 complex of the rixosome utilizes Sda1 as landing platform on nucleoplasmic pre-60S particles to wedge between the 5S rRNA tip and L1-stalk, thereby facilitating the 180° rotation of the immature 5S RNP towards its mature conformation. Upon rixosome positioning, the other sub-module with Las1 endonuclease and Grc3 polynucleotide-kinase can reach a strategic position at the pre-60S foot to cleave and 5' phosphorylate the nearby ITS2 pre-rRNA. Finally, inward movement of the L1 stalk permits the flexible Nop53 N-terminus with its AIM motif to become positioned at the base of the L1-stalk to facilitate Mtr4 helicase-exosome participation for completing ITS2 removal. Thus, the rixosome structure elucidates the coordination of two central ribosome biogenesis events, but its role in gene silencing may adapt similar strategies. PubMed: 37921038DOI: 10.15252/embr.202357984 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.8 Å) |
構造検証レポート
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