2VRH

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

Summary for 2VRH

• Entry DOI: 10.2210/pdb2vrh/pdb
• Related: 1L1P 1OMS 1P85 1P86 1P9Y 1W26 1W2B 2AW4 2AWB 2J28 2VHM 2VHN 2WWQ
• EMDB information: 1499
• Descriptor: TRIGGER FACTOR, 50S RIBOSOMAL PROTEIN L23, 50S RIBOSOMAL PROTEIN L24, ... (4 entities in total)
• Functional Keywords: 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
• Biological source: ESCHERICHIA COLI; More
• Cellular location: Cytoplasm : P0A850
• Total number of polymer chains: 4
• Total formula weight: 78488.09

Authors

Merz, F.,Boehringer, D.,Schaffitzel, C.,Preissler, S.,Hoffmann, A.,Maier, T.,Rutkowska, A.,Lozza, J.,Ban, N.,Bukau, B.,Deuerling, E. (deposition date: 2008-04-07, release date: 2008-06-17, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (19 Å)