1W2B

Trigger Factor ribosome binding domain in complex with 50S

Summary for 1W2B

• Entry DOI: 10.2210/pdb1w2b/pdb
• Related: 1FFK 1JJ2 1K73 1K8A 1K9M 1KC8 1KD1 1KQS 1M1K 1M90 1N8R 1NJI 1Q7Y 1Q81 1Q82 1Q86 1QVF 1QVG 1S72
• Descriptor: 23S RRNA, 50S RIBOSOMAL PROTEIN L6P, 50S RIBOSOMAL PROTEIN L7AE, ... (37 entities in total)
• Functional Keywords: ribosome, ribosome_associated factors, chaperone, nascent chain, cotranslational folding, rna-binding, ribosomal protein
• Biological source: ESCHERICHIA COLI; More
• Cellular location: Cytoplasm : P12743
• Total number of polymer chains: 31
• Total formula weight: 1473992.22

Authors

Ferbitz, L.,Maier, T.,Patzelt, H.,Bukau, B.,Deuerling, E.,Ban, N. (deposition date: 2004-07-01, release date: 2004-09-02, Last modification date: 2023-12-13)

Primary citation

Ferbitz, L.,Maier, T.,Patzelt, H.,Bukau, B.,Deuerling, E.,Ban, N.
Trigger Factor in Complex with the Ribosome Forms a Molecular Cradle for Nascent Proteins
Nature, 431:590-, 2004

PubMed Abstract: During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we present a 2.7 A crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding 'tail', the peptidyl-prolyl isomerase 'head', the carboxy-terminal 'arms' and connecting regions building up the 'back'. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones.

PubMed: 15334087
DOI: 10.1038/NATURE02899

Experimental method

X-RAY DIFFRACTION (3.5 Å)