7D6Z

Molecular model of the cryo-EM structure of 70S ribosome in complex with peptide deformylase and trigger factor

これはPDB形式変換不可エントリーです。

7D6Z の概要

• エントリーDOI: 10.2210/pdb7d6z/pdb
• EMDBエントリー: 30598
• 分子名称: 30S ribosomal protein S20, 50S ribosomal protein L3, 50S ribosomal protein L4, ... (58 entities in total)
• 機能のキーワード: escherichia coli, ribosome, nascent chain, protein biogenesis, peptide deformylase, trigger factor
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 2258929.54

構造登録者

Akbar, S.,Bhakta, S.,Sengupta, J. (登録日: 2020-10-02, 公開日: 2021-04-07, 最終更新日: 2024-10-16)

主引用文献

Akbar, S.,Bhakta, S.,Sengupta, J.
Structural insights into the interplay of protein biogenesis factors with the 70S ribosome.
Structure, 29:755-767.e4, 2021

PubMed Abstract: Bacterial co-translational N-terminal methionine excision, an early event of nascent polypeptide chain processing, is mediated by two enzymes: peptide deformylase (PDF) and methionine aminopeptidase (MetAP). Trigger factor (TF), the only ribosome-associated bacterial chaperone, offers co-translational chaperoning assistance. Here, we present two high-resolution cryoelectron microscopy structures of tRNA-bound E. coli ribosome complexes showing simultaneous binding of PDF and TF, in the absence (3.4 Å) and presence of MetAP (4.1 Å). These structures establish molecular details of the interactions of the factors with the ribosome, and thereby reveal the structural basis of nascent chain processing. Our results suggest that simultaneous binding of all three factors is not a functionally favorable mechanism of nascent chain processing. Strikingly, an unusual structural distortion of the 70S ribosome, potentially driven by binding of multiple copies of MetAP, is observed when MetAP is incubated with a pre-formed PDF-TF-bound ribosome complex.

PubMed: 33761323
DOI: 10.1016/j.str.2021.03.005

実験手法

ELECTRON MICROSCOPY (3.4 Å)