8HFR の概要
| エントリーDOI | 10.2210/pdb8hfr/pdb |
| EMDBエントリー | 34725 |
| 分子名称 | 60S ribosomal protein L35-A, Nucleolar GTP-binding protein 1, Ribosome biogenesis protein RLP24, ... (58 entities in total) |
| 機能のキーワード | pre-60s ribosome, ribosome |
| 由来する生物種 | Saccharomyces cerevisiae S288C 詳細 |
| タンパク質・核酸の鎖数 | 61 |
| 化学式量合計 | 2639604.44 |
| 構造登録者 | |
| 主引用文献 | Li, Z.,Chen, S.,Zhao, L.,Huang, G.,Xu, H.,Yang, X.,Wang, P.,Gao, N.,Sui, S.F. Nuclear export of pre-60S particles through the nuclear pore complex. Nature, 618:411-418, 2023 Cited by PubMed Abstract: The nuclear pore complex (NPC) is the bidirectional gate that mediates the exchange of macromolecules or their assemblies between nucleus and cytoplasm. The assembly intermediates of the ribosomal subunits, pre-60S and pre-40S particles, are among the largest cargoes of the NPC and the export of these gigantic ribonucleoproteins requires numerous export factors. Here we report the cryo-electron microscopy structure of native pre-60S particles trapped in the channel of yeast NPCs. In addition to known assembly factors, multiple factors with export functions are also included in the structure. These factors in general bind to either the flexible regions or subunit interface of the pre-60S particle, and virtually form many anchor sites for NPC binding. Through interactions with phenylalanine-glycine (FG) repeats from various nucleoporins of NPC, these factors collectively facilitate the passage of the pre-60S particle through the central FG repeat network of the NPC. Moreover, in silico analysis of the axial and radial distribution of pre-60S particles within the NPC shows that a single NPC can take up to four pre-60S particles simultaneously, and pre-60S particles are enriched in the inner ring regions close to the wall of the NPC with the solvent-exposed surface facing the centre of the nuclear pore. Our data suggest a translocation model for the export of pre-60S particles through the NPC. PubMed: 37258668DOI: 10.1038/s41586-023-06128-y 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.64 Å) |
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