2VRH

Structure of the E. coli trigger factor bound to a translating ribosome

2VRH の概要

• エントリーDOI: 10.2210/pdb2vrh/pdb
• 関連するPDBエントリー: 1L1P 1OMS 1P85 1P86 1P9Y 1W26 1W2B 2AW4 2AWB 2J28 2VHM 2VHN 2WWQ
• EMDBエントリー: 1499
• 分子名称: TRIGGER FACTOR, 50S RIBOSOMAL PROTEIN L23, 50S RIBOSOMAL PROTEIN L24, ... (4 entities in total)
• 機能のキーワード: ribosome, trigger factor, ribosomal protein, ribonucleoprotein, co-translational protein folding, rotamase, chaperone, isomerase, cell cycle, rna-binding, rrna-binding, cell division, ribosome-nascent chain complex
• 由来する生物種: ESCHERICHIA COLI; 詳細
• 細胞内の位置: Cytoplasm : P0A850
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78488.09

構造登録者

Merz, F.,Boehringer, D.,Schaffitzel, C.,Preissler, S.,Hoffmann, A.,Maier, T.,Rutkowska, A.,Lozza, J.,Ban, N.,Bukau, B.,Deuerling, E. (登録日: 2008-04-07, 公開日: 2008-06-17, 最終更新日: 2024-11-06)

主引用文献

Merz, F.,Boehringer, D.,Schaffitzel, C.,Preissler, S.,Hoffmann, A.,Maier, T.,Rutkowska, A.,Lozza, J.,Ban, N.,Bukau, B.,Deuerling, E.
Molecular Mechanism and Structure of Trigger Factor Bound to the Translating Ribosome.
Embo J., 27:1622-, 2008

PubMed Abstract: Ribosome-associated chaperone Trigger Factor (TF) initiates folding of newly synthesized proteins in bacteria. Here, we pinpoint by site-specific crosslinking the sequence of molecular interactions of Escherichia coli TF and nascent chains during translation. Furthermore, we provide the first full-length structure of TF associated with ribosome-nascent chain complexes by using cryo-electron microscopy. In its active state, TF arches over the ribosomal exit tunnel accepting nascent chains in a protective void. The growing nascent chain initially follows a predefined path through the entire interior of TF in an unfolded conformation, and even after folding into a domain it remains accommodated inside the protective cavity of ribosome-bound TF. The adaptability to accept nascent chains of different length and folding states may explain how TF is able to assist co-translational folding of all kinds of nascent polypeptides during ongoing synthesis. Moreover, we suggest a model of how TF's chaperoning function can be coordinated with the co-translational processing and membrane targeting of nascent polypeptides by other ribosome-associated factors.

PubMed: 18497744
DOI: 10.1038/EMBOJ.2008.89

実験手法

ELECTRON MICROSCOPY (19 Å)