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3JCE

Structure of Escherichia coli EF4 in pretranslocational ribosomes (Pre EF4)

これはPDB形式変換不可エントリーです。
3JCE の概要
エントリーDOI10.2210/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
Zhang, D.,Yan, K.,Liu, G.,Song, G.,Luo, J.,Shi, Y.,Cheng, E.,Wu, S.,Jiang, T.,Low, J.,Gao, N.,Qin, Y. (登録日: 2015-12-01, 公開日: 2016-01-13, 最終更新日: 2024-06-05)
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: 26809121
DOI: 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)
構造検証レポート
Validation report summary of 3jce
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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