Publikation: Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
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During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosomeassociated chaperones, which assist their folding to the native state. Here we present a 2.7A ° 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.
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FERBITZ, Lars, Timm MAIER, Holger PATZELT, Bernd BUKAU, Elke DEUERLING, Ban NENAD, 2004. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. In: Nature. 2004, 431(7008), pp. 590-596. ISSN 0028-0836. eISSN 1476-4679. Available under: doi: 10.1038/nature02899BibTex
@article{Ferbitz2004Trigg-7229, year={2004}, doi={10.1038/nature02899}, title={Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins}, number={7008}, volume={431}, issn={0028-0836}, journal={Nature}, pages={590--596}, author={Ferbitz, Lars and Maier, Timm and Patzelt, Holger and Bukau, Bernd and Deuerling, Elke and Nenad, Ban} }
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