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8A3L

Structural insights into the binding of bS1 to the ribosome

これはPDB形式変換不可エントリーです。
8A3L の概要
エントリーDOI10.2210/pdb8a3l/pdb
EMDBエントリー15116
分子名称16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total)
機能のキーワードbs1, ribosome, cryo-em, translation
由来する生物種Escherichia coli K-12
詳細
タンパク質・核酸の鎖数56
化学式量合計2265491.71
構造登録者
D'Urso, G.,Chat, S.,Gillet, R.,Giudice, E. (登録日: 2022-06-08, 公開日: 2023-05-10, 最終更新日: 2025-12-24)
主引用文献D'Urso, G.,Chat, S.,Gillet, R.,Giudice, E.
Structural insights into the binding of bS1 to the ribosome.
Nucleic Acids Res., 51:3410-3419, 2023
Cited by
PubMed Abstract: The multidomain ribosomal protein bS1 is the biggest and the most flexible and dynamic protein in the 30S small subunit. Despite being essential for mRNA recruitment and its primary role in the accommodation of the start codon within the decoding centre, there has not yet been a high-resolution description of its structure. Here, we present a 3D atomic model of OB1 and OB2, bS1's first two N-terminal domains, bound to an elongation-competent 70S ribosome. Our structure reveals that, as previously reported, bS1 is anchored both by a π-stacking to the 30S subunit and via a salt bridge with the Zn2+ pocket of bS1. These contacts are further stabilized by other interactions with additional residues on OB1. Our model also shows a new conformation of OB2, interacting with the Shine-Dalgarno portion of the mRNA. This study confirms that OB1 plays an anchoring role, but also highlights a novel function for OB2, which is directly involved in the modulation and support of mRNA binding and accommodation on the ribosome.
PubMed: 36840711
DOI: 10.1093/nar/gkad126
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.42 Å)
構造検証レポート
Validation report summary of 8a3l
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2026-01-28に公開中

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