PMID:15334087
| Citation |
Ferbitz, L, Maier, T, Patzelt, H, Bukau, B, Deuerling, E and Ban, N (2004) Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431:590-6 |
|---|---|
| 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 A 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. |
| Links |
PubMed Online version:10.1038/nature02899 |
| Keywords |
Crystallization; Crystallography, X-Ray; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Haloarcula marismortui; Hydrophobic and Hydrophilic Interactions; Models, Genetic; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Peptidylprolyl Isomerase/chemistry; Peptidylprolyl Isomerase/metabolism; Protein Binding; Protein Biosynthesis; Protein Conformation; Protein Folding; Protein Subunits/chemistry; Protein Subunits/metabolism; Proteins/chemistry; Proteins/metabolism; Ribosomes/chemistry; Ribosomes/metabolism |
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