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
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/nature02899 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:431:y:2004:i:7008:d:10.1038_nature02899

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature02899

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().