5LMT
Structure of bacterial 30S-IF1-IF3-mRNA-tRNA translation pre-initiation complex(state-3)
5LMT の概要
| エントリーDOI | 10.2210/pdb5lmt/pdb |
| EMDBエントリー | 4079 |
| 分子名称 | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (27 entities in total) |
| 機能のキーワード | ribosome, translation, initiation factors, 30s, if1, if3, trnai, pic, thermus thermophilus |
| 由来する生物種 | Thermus thermophilus HB8 詳細 |
| タンパク質・核酸の鎖数 | 25 |
| 化学式量合計 | 852095.67 |
| 構造登録者 | Hussain, T.,Llacer, J.L.,Wimberly, B.T.,Ramakrishnan, V. (登録日: 2016-08-01, 公開日: 2016-10-05, 最終更新日: 2025-12-17) |
| 主引用文献 | Hussain, T.,Llacer, J.L.,Wimberly, B.T.,Kieft, J.S.,Ramakrishnan, V. Large-Scale Movements of IF3 and tRNA during Bacterial Translation Initiation. Cell, 167:133-144.e13, 2016 Cited by PubMed Abstract: In bacterial translational initiation, three initiation factors (IFs 1-3) enable the selection of initiator tRNA and the start codon in the P site of the 30S ribosomal subunit. Here, we report 11 single-particle cryo-electron microscopy (cryoEM) reconstructions of the complex of bacterial 30S subunit with initiator tRNA, mRNA, and IFs 1-3, representing different steps along the initiation pathway. IF1 provides key anchoring points for IF2 and IF3, thereby enhancing their activities. IF2 positions a domain in an extended conformation appropriate for capturing the formylmethionyl moiety charged on tRNA. IF3 and tRNA undergo large conformational changes to facilitate the accommodation of the formylmethionyl-tRNA (fMet-tRNA(fMet)) into the P site for start codon recognition. PubMed: 27662086DOI: 10.1016/j.cell.2016.08.074 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.15 Å) |
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