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-Structure paper
タイトル | Structural insights into the binding of bS1 to the ribosome. |
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ジャーナル・号・ページ | Nucleic Acids Res, Vol. 51, Issue 7, Page 3410-3419, Year 2023 |
掲載日 | 2023年4月24日 |
著者 | Gaetano D'Urso / Sophie Chat / Reynald Gillet / Emmanuel Giudice / |
PubMed 要旨 | 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 ...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. |
リンク | Nucleic Acids Res / PubMed:36840711 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.42 Å |
構造データ | EMDB-15116, PDB-8a3l: |
化合物 | ChemComp-MG: ChemComp-ZN: |
由来 |
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キーワード | RIBOSOME / bS1 / Cryo-EM / Translation |