5LZS

Structure of the mammalian ribosomal elongation complex with aminoacyl-tRNA, eEF1A, and didemnin B

これはPDB形式変換不可エントリーです。

5LZS の概要

• エントリーDOI: 10.2210/pdb5lzs/pdb
• EMDBエントリー: 4130
• 分子名称: uL2, uL5, eL13, ... (89 entities in total)
• 機能のキーワード: translation, elongation, ribosome
• 由来する生物種: Oryctolagus cuniculus (Rabbit); 詳細
• タンパク質・核酸の鎖数: 86
• 化学式量合計: 3496475.49

構造登録者

Shao, S.,Murray, J.,Brown, A.,Taunton, J.,Ramakrishnan, V.,Hegde, R.S. (登録日: 2016-10-02, 公開日: 2016-11-30, 最終更新日: 2019-12-11)

主引用文献

Shao, S.,Murray, J.,Brown, A.,Taunton, J.,Ramakrishnan, V.,Hegde, R.S.
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.
Cell, 167:1229-1240.e15, 2016

PubMed Abstract: In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factor⋅GTPase complexes representing intermediates of translation elongation (aminoacyl-tRNA⋅eEF1A), termination (eRF1⋅eRF3), and ribosome rescue (Pelota⋅Hbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factor⋅GTPase complex to ensure translational fidelity.

PubMed: 27863242
DOI: 10.1016/j.cell.2016.10.046

実験手法

ELECTRON MICROSCOPY (3.31 Å)