5M6S

folding intermediate of spectrin R16

5M6S の概要

• エントリーDOI: 10.2210/pdb5m6s/pdb
• EMDBエントリー: 3451
• 分子名称: spectrin (1 entity in total)
• 機能のキーワード: spectrin, r16, structural protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19370.60

構造登録者

Nilsson, O.B.,Nickson, A.A.,Clarke, J. (登録日: 2016-10-25, 公開日: 2017-01-11, 最終更新日: 2024-05-08)

主引用文献

Nilsson, O.B.,Nickson, A.A.,Hollins, J.J.,Wickles, S.,Steward, A.,Beckmann, R.,von Heijne, G.,Clarke, J.
Cotranslational folding of spectrin domains via partially structured states.
Nat. Struct. Mol. Biol., 24:221-225, 2017

PubMed Abstract: How do the key features of protein folding, elucidated from studies on native, isolated proteins, manifest in cotranslational folding on the ribosome? Using a well-characterized family of homologous α-helical proteins with a range of biophysical properties, we show that spectrin domains can fold vectorially on the ribosome and may do so via a pathway different from that of the isolated domain. We use cryo-EM to reveal a folded or partially folded structure, formed in the vestibule of the ribosome. Our results reveal that it is not possible to predict which domains will fold within the ribosome on the basis of the folding behavior of isolated domains; instead, we propose that a complex balance of the rate of folding, the rate of translation and the lifetime of folded or partly folded states will determine whether folding occurs cotranslationally on actively translating ribosomes.

PubMed: 28112730
DOI: 10.1038/nsmb.3355

実験手法

ELECTRON MICROSCOPY (4.8 Å)