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Chaperone binding at the ribosomal exit tunnel.
Ole Kristensen1, Michael Gajhede
1Structural Biology, Department of Medicinal Chemistry, The Danish University of Pharmaceutical Sciences, Universitetsparken 2, DK-2100 Copenhagen, Denmark. ok@dfh.dk
Structure (London, England : 1993)
|December 6, 2003
Summary
Chaperone trigger factor (TF) binds the ribosome via its N-terminal domain for efficient protein folding. Crystal structures reveal a unique helical kink critical for TF
Area of Science:
- Molecular biology
- Structural biology
- Biochemistry
Background:
- The ribosome's exit tunnel is key for nascent polypeptide interactions.
- Chaperone trigger factor (TF) binds the 50S ribosomal subunit for protein folding.
- Signal recognition particle (SRP) also couples to translation for protein translocation.
Purpose of the Study:
- To elucidate the structural basis of trigger factor (TF) ribosome association.
- To compare the TF ribosome binding domain with related chaperone structures.
Main Methods:
- X-ray crystallography of the E. coli TF ribosome binding domain.
Main Results:
- TF possesses a prominent ribosome anchor at its tip, including a unique signature motif.
- This TF anchor differs structurally from features observed in SRP.
- A conserved helical kink was identified as a hallmark of the TF structure.
Conclusions:
- The identified helical kink is likely essential for stable trigger factor (TF) ribosome association.
- Structural insights advance understanding of chaperone-ribosome interactions in protein folding.