3JCE の概要
エントリーDOI | 10.2210/pdb3jce/pdb |
関連するPDBエントリー | 3jcd |
EMDBエントリー | 6550 |
分子名称 | 16S ribosomal RNA, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (60 entities in total) |
機能のキーワード | ribosome elongation, gtpase ef4, trna back-translocation, p-loop, ribosome |
由来する生物種 | Escherichia coli K-12 詳細 |
タンパク質・核酸の鎖数 | 58 |
化学式量合計 | 2314955.60 |
構造登録者 | |
主引用文献 | Zhang, D.,Yan, K.,Liu, G.,Song, G.,Luo, J.,Shi, Y.,Cheng, E.,Wu, S.,Jiang, T.,Lou, J.,Gao, N.,Qin, Y. EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome Nat. Struct. Mol. Biol., 23:125-131, 2016 Cited by PubMed Abstract: EF4 catalyzes tRNA back-translocation through an unknown mechanism. We report cryo-EM structures of Escherichia coli EF4 in post- and pretranslocational ribosomes (Post- and Pre-EF4) at 3.7- and 3.2-Å resolution, respectively. In Post-EF4, peptidyl-tRNA occupies the peptidyl (P) site, but the interaction between its CCA end and the P loop is disrupted. In Pre-EF4, the peptidyl-tRNA assumes a unique position near the aminoacyl (A) site, denoted the A site/EF4 bound (A/4) site, with a large displacement at its acceptor arm. Mutagenesis analyses suggest that a specific region in the EF4 C-terminal domain (CTD) interferes with base-pairing between the peptidyl-tRNA 3'-CCA and the P loop, whereas the EF4 CTD enhances peptidyl-tRNA interaction at the A/4 site. Therefore, EF4 induces back-translocation by disengaging the tRNA's CCA end from the peptidyl transferase center of the translating ribosome. PubMed: 26809121DOI: 10.1038/nsmb.3160 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
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