1P9Y

Ribosome binding of E. coli Trigger Factor mutant F44L.

Summary for 1P9Y

• Entry DOI: 10.2210/pdb1p9y/pdb
• Related: 1OMS
• Descriptor: Trigger factor, ACETIC ACID (3 entities in total)
• Functional Keywords: alpha-beta protein, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 26840.57

Authors

Kristensen, O.,Gajhede, M. (deposition date: 2003-05-13, release date: 2003-12-16, Last modification date: 2023-10-25)

Primary citation

Kristensen, O.,Gajhede, M.
Chaperone binding at the ribosomal exit tunnel.
Structure, 11:1547-1556, 2003

PubMed 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.

PubMed: 14656439
DOI: 10.1016/j.str.2003.11.003

Experimental method

X-RAY DIFFRACTION (2.15 Å)