4WJV
Crystal structure of Rsa4 in complex with the Nsa2 binding peptide
4WJV の概要
| エントリーDOI | 10.2210/pdb4wjv/pdb |
| 関連するPDBエントリー | 4WJU |
| 関連するBIRD辞書のPRD_ID | PRD_900001 |
| 分子名称 | Ribosome assembly protein 4, Maltose-binding periplasmic protein, Ribosome biogenesis protein NSA2, ... (5 entities in total) |
| 機能のキーワード | ribosome biogenesis ribosome assembly, protein binding |
| 由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) 詳細 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 348677.54 |
| 構造登録者 | Holdermann, I.,Paternoga, H.,Bassler, J.,Hurt, E.,Sinning, I. (登録日: 2014-10-01, 公開日: 2014-11-19, 最終更新日: 2024-01-10) |
| 主引用文献 | Baler, J.,Paternoga, H.,Holdermann, I.,Thoms, M.,Granneman, S.,Barrio-Garcia, C.,Nyarko, A.,Stier, G.,Clark, S.A.,Schraivogel, D.,Kallas, M.,Beckmann, R.,Tollervey, D.,Barbar, E.,Sinning, I.,Hurt, E. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. J.Cell Biol., 207:481-498, 2014 Cited by PubMed Abstract: Eukaryotic ribosome biogenesis involves ∼200 assembly factors, but how these contribute to ribosome maturation is poorly understood. Here, we identify a network of factors on the nascent 60S subunit that actively remodels preribosome structure. At its hub is Rsa4, a direct substrate of the force-generating ATPase Rea1. We show that Rsa4 is connected to the central protuberance by binding to Rpl5 and to ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2. Importantly, Nsa2 binds to helix 89 before relocation of helix 89 to the PTC. Structure-based mutations of these factors reveal the functional importance of their interactions for ribosome assembly. Thus, Rsa4 is held tightly in the preribosome and can serve as a "distribution box," transmitting remodeling energy from Rea1 into the developing ribosome. We suggest that a relay-like factor network coupled to a mechano-enzyme is strategically positioned to relocate rRNA elements during ribosome maturation. PubMed: 25404745DOI: 10.1083/jcb.201408111 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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