- EMDB-2695: Cryo-EM map of Trigger Factor bound to a translating ribosome -
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基本情報
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データベース: EMDB / ID: EMD-2695
タイトル
Cryo-EM map of Trigger Factor bound to a translating ribosome
マップデータ
High resolution map of ribosome-bound Trigger Factor
試料
試料: TnaC-stalled-RNC with Trigger factor
複合体: cytosolic 70S ribosome
タンパク質・ペプチド: Trigger factor
キーワード
translation / co-translational protein folding
機能・相同性
機能・相同性情報
'de novo' cotranslational protein folding / stress response to copper ion / protein unfolding / protein folding chaperone / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein transport / response to heat / protein folding / ribosome binding ...'de novo' cotranslational protein folding / stress response to copper ion / protein unfolding / protein folding chaperone / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein transport / response to heat / protein folding / ribosome binding / cell division / membrane / identical protein binding / cytosol 類似検索 - 分子機能
ジャーナル: J Mol Biol / 年: 2016 タイトル: Dynamic Behavior of Trigger Factor on the Ribosome. 著者: J Deeng / K Y Chan / E O van der Sluis / O Berninghausen / W Han / J Gumbart / K Schulten / B Beatrix / R Beckmann / 要旨: Trigger factor (TF) is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chain (NCs) as they emerge from the ribosome. TF binds via its N-terminal ...Trigger factor (TF) is the only ribosome-associated chaperone in bacteria. It interacts with hydrophobic segments in nascent chain (NCs) as they emerge from the ribosome. TF binds via its N-terminal ribosome-binding domain (RBD) mainly to ribosomal protein uL23 at the tunnel exit on the large ribosomal subunit. Whereas earlier structural data suggested that TF binds as a rigid molecule to the ribosome, recent comparisons of structural data on substrate-bound, ribosome-bound, and TF in solution from different species suggest that this chaperone is a rather flexible molecule. Here, we present two cryo-electron microscopy structures of TF bound to ribosomes translating an mRNA coding for a known TF substrate from Escherichia coli of a different length. The structures reveal distinct degrees of flexibility for the different TF domains, a conformational rearrangement of the RBD upon ribosome binding, and an increase in rigidity within TF when the NC is extended. Molecular dynamics simulations agree with these data and offer a molecular basis for these observations.