5A7U

Single-particle cryo-EM of co-translational folded adr1 domain inside the E. coli ribosome exit tunnel.

5A7U の概要

• エントリーDOI: 10.2210/pdb5a7u/pdb
• EMDBエントリー: 3079
• 分子名称: REGULATORY PROTEIN ADR1, ZINC ION (2 entities in total)
• 機能のキーワード: protein folding, translation, ribosome, zinc finger, secm, translational arrest peptide, cryo-em, single- molecule studies
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Nucleus: P07248
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3471.43

構造登録者

Nilsson, O.B.,Hedman, R.,Marino, J.,Wickles, S.,Bischoff, L.,Johansson, M.,Muller-Lucks, A.,Trovato, F.,Puglisi, J.D.,O'Brien, E.,Beckmann, R.,von Heijne, G. (登録日: 2015-07-10, 公開日: 2015-09-16, 最終更新日: 2024-05-08)

主引用文献

Nilsson, O.B.,Hedman, R.,Marino, J.,Wickles, S.,Bischoff, L.,Johansson, M.,Muller-Lucks, A.,Trovato, F.,Puglisi, J.D.,O'Brien, E.P.,Beckmann, R.,Von Heijne, G.
Cotranslational Protein Folding Inside the Ribosome Exit Tunnel.
Cell Rep., 12:1533-, 2015

PubMed Abstract: At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.

PubMed: 26321634
DOI: 10.1016/J.CELREP.2015.07.065

実験手法

ELECTRON MICROSCOPY (4.8 Å)