9P76 の概要
| エントリーDOI | 10.2210/pdb9p76/pdb |
| EMDBエントリー | 71333 |
| 分子名称 | Transcription factor BTF3, Large ribosomal subunit protein uL4, Large ribosomal subunit protein uL18, ... (89 entities in total) |
| 機能のキーワード | in situ, ribosome |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 85 |
| 化学式量合計 | 3304790.17 |
| 構造登録者 | |
| 主引用文献 | Zheng, W.,Zhang, Y.,Wang, J.,Wang, S.,Chai, P.,Bailey, E.J.,Zhu, C.,Guo, W.,Devarkar, S.C.,Wu, S.,Lin, J.,Zhang, K.,Liu, J.,Lomakin, I.B.,Xiong, Y. Visualizing the translation landscape in human cells at high resolution. Nat Commun, 16:10757-10757, 2025 Cited by PubMed Abstract: Comprehensive in situ structures of macromolecules can transform our understanding of biology and advance human health. Here, we map protein synthesis inside human cells in detail by combining automated cryo-focused ion beam (FIB) milling and in situ single-particle cryo electron microscopy (cryo-EM). With this in situ cryo-EM approach, we resolved a 2.2 Å consensus structure of the human 80S ribosome and unveiled 23 functional states, nearly all better than 3 Å resolution. Compared to in vitro studies, we observed variations in ribosome structures, distinct environments of ion and polyamine binding, and associated proteins such as EDF1 and NACβ that are typically not enriched with purified ribosomes. We also detected additional peptide-related density features on the ribosome and visualized ribosome-ribosome interactions in helical polysomes. Finally, high-resolution structures from cells treated with homoharringtonine and cycloheximide revealed a distinct translational landscape and a spermidine that interacts with cycloheximide at the E site, one of the numerous polyamines that also bind native ribosomes. These results underscore the value of high-resolution in situ studies in the native environment. PubMed: 41315256DOI: 10.1038/s41467-025-65795-9 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.83 Å) |
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