6ENU6ENU の概要
| エントリーDOI | 10.2210/pdb6enu/pdb |
| 関連するPDBエントリー | 6ENF 6ENJ |
| EMDBエントリー | 3903 |
| 分子名称 | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total) |
| 機能のキーワード | proline, ef-p, ribosome, nascent chain, stalling |
| 由来する生物種 | Escherichia coli 詳細 |
| 細胞内の位置 | Cytoplasm: P0A6N4 |
| タンパク質・核酸の鎖数 | 56 |
| 化学式量合計 | 2183666.49 |
| 構造登録者 | |
| 主引用文献 | Huter, P.,Arenz, S.,Bock, L.V.,Graf, M.,Frister, J.O.,Heuer, A.,Peil, L.,Starosta, A.L.,Wohlgemuth, I.,Peske, F.,Novacek, J.,Berninghausen, O.,Grubmuller, H.,Tenson, T.,Beckmann, R.,Rodnina, M.V.,Vaiana, A.C.,Wilson, D.N. Structural Basis for Polyproline-Mediated Ribosome Stalling and Rescue by the Translation Elongation Factor EF-P. Mol. Cell, 68:515-527.e6, 2017 Cited by PubMed Abstract: Ribosomes synthesizing proteins containing consecutive proline residues become stalled and require rescue via the action of uniquely modified translation elongation factors, EF-P in bacteria, or archaeal/eukaryotic a/eIF5A. To date, no structures exist of EF-P or eIF5A in complex with translating ribosomes stalled at polyproline stretches, and thus structural insight into how EF-P/eIF5A rescue these arrested ribosomes has been lacking. Here we present cryo-EM structures of ribosomes stalled on proline stretches, without and with modified EF-P. The structures suggest that the favored conformation of the polyproline-containing nascent chain is incompatible with the peptide exit tunnel of the ribosome and leads to destabilization of the peptidyl-tRNA. Binding of EF-P stabilizes the P-site tRNA, particularly via interactions between its modification and the CCA end, thereby enforcing an alternative conformation of the polyproline-containing nascent chain, which allows a favorable substrate geometry for peptide bond formation. PubMed: 29100052DOI: 10.1016/j.molcel.2017.10.014 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
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