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4WJU

Crystal structure of Rsa4 from Saccharomyces cerevisiae

4WJU の概要
エントリーDOI10.2210/pdb4wju/pdb
関連するPDBエントリー4WJS
分子名称Ribosome assembly protein 4, GLYCEROL (2 entities in total)
機能のキーワードribosome biogenesis ribosome assembly, biosynthetic protein
由来する生物種Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
詳細
細胞内の位置Nucleus, nucleolus : P25382
タンパク質・核酸の鎖数2
化学式量合計114305.66
構造登録者
Holdermann, I.,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: 25404745
DOI: 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 (2.8 Å)
構造検証レポート
Validation report summary of 4wju
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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