6OST の概要
| エントリーDOI | 10.2210/pdb6ost/pdb |
| EMDBエントリー | 20188 |
| 分子名称 | 23S Ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (57 entities in total) |
| 機能のキーワード | time-resolved cryo-em, termination, short-lived, millisecond, ribosome |
| 由来する生物種 | Escherichia coli 詳細 |
| タンパク質・核酸の鎖数 | 55 |
| 化学式量合計 | 2175760.62 |
| 構造登録者 | Fu, Z.,Indrisiunaite, G.,Kaledhonkar, S.,Shah, B.,Sun, M.,Chen, B.,Grassucci, R.A.,Ehrenberg, M.,Frank, J. (登録日: 2019-05-02, 公開日: 2019-06-19, 最終更新日: 2025-03-19) |
| 主引用文献 | Fu, Z.,Indrisiunaite, G.,Kaledhonkar, S.,Shah, B.,Sun, M.,Chen, B.,Grassucci, R.A.,Ehrenberg, M.,Frank, J. The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy. Nat Commun, 10:2579-2579, 2019 Cited by PubMed Abstract: When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms. PubMed: 31189921DOI: 10.1038/s41467-019-10608-z 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.2 Å) |
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