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6FU8

uL23 beta hairpin loop deletion of E.coli ribosome

6FU8 の概要
エントリーDOI10.2210/pdb6fu8/pdb
EMDBエントリー4319
分子名称50S ribosomal protein L23 (1 entity in total)
機能のキーワードul23, loop deletion, ribosomal tunnel, ribosomal protein
由来する生物種Escherichia coli O157:H7
タンパク質・核酸の鎖数1
化学式量合計9324.00
構造登録者
Kudva, R.,von Heijne, G.,Carroni, M. (登録日: 2018-02-26, 公開日: 2018-12-05, 最終更新日: 2024-05-15)
主引用文献Kudva, R.,Tian, P.,Pardo-Avila, F.,Carroni, M.,Best, R.B.,Bernstein, H.D.,von Heijne, G.
The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding.
Elife, 7:-, 2018
Cited by
PubMed Abstract: The ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 Δloop ribosomes, while two ~ 100 residue proteins normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 Δloop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure.
PubMed: 30475203
DOI: 10.7554/eLife.36326
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.2 Å)
構造検証レポート
Validation report summary of 6fu8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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