Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Lars Ferbitz,
Timm Maier,
Holger Patzelt,
Bernd Bukau,
Elke Deuerling () and
Nenad Ban ()
Additional contact information
Lars Ferbitz: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)
Timm Maier: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)
Holger Patzelt: Universität Heidelberg
Bernd Bukau: Universität Heidelberg
Elke Deuerling: Universität Heidelberg
Nenad Ban: Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich)
Nature, 2004, vol. 431, issue 7008, 590-596
Abstract:
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 state1,2. Here we present a 2.7 Å 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.
Date: 2004
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:431:y:2004:i:7008:d:10.1038_nature02899
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DOI: 10.1038/nature02899
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