Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Ferbitz, L. and Maier, Timm and Patzelt, H. and Bukau, B. and Deuerling, E. and Ban, N.. (2004) Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature, 431 (7008). pp. 590-596.

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Official URL: http://edoc.unibas.ch/45827/

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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(1,2). Here we present a 2.7 Angstrom 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 peptidylprolyl 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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:03 Nov 2017 11:26
Deposited On:03 Nov 2017 11:26

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