7OT5

CspA-70 cotranslational folding intermediate 1

これはPDB形式変換不可エントリーです。

7OT5 の概要

• エントリーDOI: 10.2210/pdb7ot5/pdb
• EMDBエントリー: 13055
• 分子名称: 23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (57 entities in total)
• 機能のキーワード: cotranslational folding, cspa70-1, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 2160803.02

構造登録者

Agirrezabala, X.,Samatova, E.,Macher, M.,Liutkute, M.,Gil-Carton, D.,Novacek, J.,Valle, M.,Rodnina, M.V. (登録日: 2021-06-09, 公開日: 2022-01-19, 最終更新日: 2025-03-12)

主引用文献

Agirrezabala, X.,Samatova, E.,Macher, M.,Liutkute, M.,Maiti, M.,Gil-Carton, D.,Novacek, J.,Valle, M.,Rodnina, M.V.
A switch from alpha-helical to beta-strand conformation during co-translational protein folding.
Embo J., 41:e109175-e109175, 2022

PubMed Abstract: Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent chains is not only shaped by their amino acid sequence but also by the interactions with the ribosome. Here, we combine biophysical methods with cryo-EM structure determination to show that folding of a β-barrel protein begins with formation of a dynamic α-helix inside the ribosome. As the growing peptide reaches the end of the tunnel, the N-terminal part of the nascent chain refolds to a β-hairpin structure that remains dynamic until its release from the ribosome. Contacts with the ribosome and structure of the peptidyl transferase center depend on nascent chain conformation. These results indicate that proteins may start out as α-helices inside the tunnel and switch into their native folds only as they emerge from the ribosome. Moreover, the correlation of nascent chain conformations with reorientation of key residues of the ribosomal peptidyl-transferase center suggest that protein folding could modulate ribosome activity.

PubMed: 34994471
DOI: 10.15252/embj.2021109175

実験手法

ELECTRON MICROSCOPY (2.9 Å)