5AFF
Symportin 1 chaperones 5S RNP assembly during ribosome biogenesis by occupying an essential rRNA binding site
5AFF の概要
エントリーDOI | 10.2210/pdb5aff/pdb |
分子名称 | SYMPORTIN 1, RIBOSOMAL PROTEIN L5, RIBOSOMAL PROTEIN L11 (3 entities in total) |
機能のキーワード | chaperone, ribosome biogenesis, alpha solenoid. |
由来する生物種 | CHAETOMIUM THERMOPHILUM 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 98341.47 |
構造登録者 | Calvino, F.R.,Kharde, S.,Wild, K.,Bange, G.,Sinning, I. (登録日: 2015-01-21, 公開日: 2015-04-15, 最終更新日: 2024-01-10) |
主引用文献 | Calvino, F.R.,Kharde, S.,Ori, A.,Hendricks, A.,Wild, K.,Kressler, D.,Bange, G.,Hurt, E.,Beck, M.,Sinning, I. Symportin 1 Chaperones 5S Rnp Assembly During Ribosome Biogenesis by Occupying an Essential Rrna-Binding Site. Nat.Commun., 6:6510-, 2015 Cited by PubMed Abstract: During 60S biogenesis, mature 5S RNP consisting of 5S RNA, RpL5 and RpL11, assembles into a pre-60S particle, where docking relies on RpL11 interacting with helix 84 (H84) of the 25S RNA. How 5S RNP is assembled for recruitment into the pre-60S is not known. Here we report the crystal structure of a ternary symportin Syo1-RpL5-N-RpL11 complex and provide biochemical and structural insights into 5S RNP assembly. Syo1 guards the 25S RNA-binding surface on RpL11 and competes with H84 for binding. Pull-down experiments show that H84 releases RpL11 from the ternary complex, but not in the presence of 5S RNA. Crosslinking mass spectrometry visualizes structural rearrangements on incorporation of 5S RNA into the Syo1-RpL5-RpL11 complex supporting the formation of a pre-5S RNP. Our data underline the dual role of Syo1 in ribosomal protein transport and as an assembly platform for 5S RNP. PubMed: 25849277DOI: 10.1038/NCOMMS7510 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.398 Å) |
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