@article{db790523932046b19be04639b97bcdea,
title = "Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins",
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 state. Here we present a 2.7 {\AA} 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.",
author = "Lars Ferbitz and Timm Maier and Holgar Patzelt and Bernd Bukau and Eike Deuerling and Nenad Ban",
note = "Funding Information: Acknowledgements We thank the HHMI staff and colleagues at UMBC for technical support. This research was supported by a grant from the NIH to M.F.S. Funding Information: Acknowledgements Data collection was performed at the Swiss Light Source, Paul Scherrer Institut, Villigen and at the Swiss Norwegian Beamline (ESRF, Grenoble). We are grateful to C. Schulze-Briese, T. Tomizaki and A. Wagner at the SLS as well as P. Pattison and S. Capelli at the SNBL whose outstanding efforts have made these experiments possible. We also thank our colleagues S. Antolic, M. Steiner and members of the Ban laboratory for help in ribosome preparations and suggestions; and members of the Bukau laboratory for discussions. This work was supported by the Swiss National Science Foundation (SNSF), the NCCR Structural Biology program of the SNSF, an ETH research grant, grants of the Deutsche Forschungsgemeinschaft to B.B. and E.D. and a Young Investigator grant from the Human Frontier Science Program to N.B. and E.D.",
year = "2004",
month = sep,
day = "30",
doi = "10.1038/nature02899",
language = "English",
volume = "431",
pages = "590--596",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Research",
number = "7008",
}