6GSM
Structure of a partial yeast 48S preinitiation complex in open conformation.
これはPDB形式変換不可エントリーです。
「3JAQ」から置き換えられました6GSM の概要
| エントリーDOI | 10.2210/pdb6gsm/pdb |
| 関連するPDBエントリー | 3JAP 3JAQ |
| EMDBエントリー | 0057 3048 3049 |
| 分子名称 | Met-tRNAi, 40S ribosomal protein S6, 40S ribosomal protein S7, ... (51 entities in total) |
| 機能のキーワード | ribosome, translation, initiation factors, 40s, eif1a, eif3, eif2, trnai, 48s pic, small ribosome subunit |
| 由来する生物種 | Saccharomyces cerevisiae S288C 詳細 |
| タンパク質・核酸の鎖数 | 47 |
| 化学式量合計 | 1532958.88 |
| 構造登録者 | Llacer, J.L.,Hussain, T.,Gordiyenko, Y.,Ramakrishnan, V. (登録日: 2018-06-14, 公開日: 2019-07-31, 最終更新日: 2024-09-25) |
| 主引用文献 | Llacer, J.L.,Hussain, T.,Dong, J.,Villamayor, L.,Gordiyenko, Y.,Hinnebusch, A.G. Large-scale movement of eIF3 domains during translation initiation modulate start codon selection. Nucleic Acids Res., 2021 Cited by PubMed Abstract: The eukaryotic initiation factor 3 (eIF3) complex is involved in every step of translation initiation, but there is limited understanding of its molecular functions. Here, we present a single particle electron cryomicroscopy (cryo-EM) reconstruction of yeast 48S ribosomal preinitiation complex (PIC) in an open conformation conducive to scanning, with core subunit eIF3b bound on the 40S interface near the decoding center in contact with the ternary complex eIF2·GTP·initiator tRNA. eIF3b is relocated together with eIF3i from their solvent interface locations observed in other PIC structures, with eIF3i lacking 40S contacts. Re-processing of micrographs of our previous 48S PIC in a closed state also suggests relocation of the entire eIF3b-3i-3g-3a-Cter module during the course of initiation. Genetic analysis indicates that high fidelity initiation depends on eIF3b interactions at the 40S subunit interface that promote the closed PIC conformation, or facilitate the relocation of eIF3b/eIF3i to the solvent interface, on start codon selection. PubMed: 34648019DOI: 10.1093/nar/gkab908 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (5.15 Å) |
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