1W26

Trigger Factor in Complex with the Ribosome forms a Molecular Cradle for Nascent Proteins

Summary for 1W26

• Entry DOI: 10.2210/pdb1w26/pdb
• Related: 1L1P 1OMS 1P9Y
• Descriptor: TRIGGER FACTOR (2 entities in total)
• Functional Keywords: chaperone, protein folding, ribosome associated protein, nascent chain, cell division, isomerase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 97542.82

Authors

Ferbitz, L.,Maier, T.,Patzelt, H.,Bukau, B.,Deuerling, E.,Ban, N. (deposition date: 2004-06-28, release date: 2004-09-02, Last modification date: 2024-10-16)

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 (2.7 Å)