PMID:14656439
| Citation |
Kristensen, O and Gajhede, M (2003) Chaperone binding at the ribosomal exit tunnel. Structure 11:1547-56 |
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| Abstract |
The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association. |
| Links | |
| Keywords |
Amino Acid Motifs; Amino Acid Sequence; Crystallography, X-Ray; Dimerization; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Models, Molecular; Molecular Sequence Data; Peptidylprolyl Isomerase/chemistry; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Ribosomes/chemistry; Sequence Homology, Amino Acid; Signal Recognition Particle/chemistry |
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