@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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    <dc:contributor>Patzelt, Holger</dc:contributor>
    <dc:contributor>Ferbitz, Lars</dc:contributor>
    <dc:creator>Maier, Timm</dc:creator>
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    <dc:contributor>Maier, Timm</dc:contributor>
    <dc:creator>Bukau, Bernd</dc:creator>
    <dcterms:issued>2004</dcterms:issued>
    <dcterms:title>Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins</dcterms:title>
    <dc:language>eng</dc:language>
    <dc:contributor>Nenad, Ban</dc:contributor>
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    <dcterms:bibliographicCitation>First publ. in: Nature 431 (2004), pp. 590-596</dcterms:bibliographicCitation>
    <dc:creator>Ferbitz, Lars</dc:creator>
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    <dc:creator>Nenad, Ban</dc:creator>
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    <dc:creator>Deuerling, Elke</dc:creator>
    <dc:contributor>Deuerling, Elke</dc:contributor>
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    <dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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