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-Structure paper
タイトル | Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 Å resolution. |
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ジャーナル・号・ページ | Nucleic Acids Res, Vol. 51, Issue 8, Page 4043-4054, Year 2023 |
掲載日 | 2023年5月8日 |
著者 | Simone Pellegrino / Kyle C Dent / Tobias Spikes / Alan J Warren / |
PubMed 要旨 | The chemical modification of ribosomal RNA and proteins is critical for ribosome assembly, for protein synthesis and may drive ribosome specialisation in development and disease. However, the ...The chemical modification of ribosomal RNA and proteins is critical for ribosome assembly, for protein synthesis and may drive ribosome specialisation in development and disease. However, the inability to accurately visualise these modifications has limited mechanistic understanding of the role of these modifications in ribosome function. Here we report the 2.15 Å resolution cryo-EM reconstruction of the human 40S ribosomal subunit. We directly visualise post-transcriptional modifications within the 18S rRNA and four post-translational modifications of ribosomal proteins. Additionally, we interpret the solvation shells in the core regions of the 40S ribosomal subunit and reveal how potassium and magnesium ions establish both universally conserved and eukaryote-specific coordination to promote the stabilisation and folding of key ribosomal elements. This work provides unprecedented structural details for the human 40S ribosomal subunit that will serve as an important reference for unravelling the functional role of ribosomal RNA modifications. |
リンク | Nucleic Acids Res / PubMed:36951107 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.09 - 2.24 Å |
構造データ | EMDB-14317, PDB-7r4x: EMDB-14318: Cryo-EM reconstruction of the human 40S ribosomal subunit - Body domain EMDB-14319: Cryo-EM reconstruction of the human 40S ribosomal subunit - Head domain |
化合物 | ChemComp-K: ChemComp-MG: ChemComp-ZN: ChemComp-HOH: |
由来 |
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キーワード | RIBOSOME / rRNA modifications / post-translational modifications / cryo-EM |