6FU8
uL23 beta hairpin loop deletion of E.coli ribosome
6FU8 の概要
エントリーDOI | 10.2210/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 | |
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: 30475203DOI: 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) |
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