1p9y
From Proteopedia
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| , resolution 2.15Å | |||||||
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| Ligands: | |||||||
| Gene: | TIG (Escherichia coli) | ||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Related: | 1OMS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ribosome binding of E. coli Trigger Factor mutant F44L.
Overview
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.
About this Structure
1P9Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Chaperone binding at the ribosomal exit tunnel., Kristensen O, Gajhede M, Structure. 2003 Dec;11(12):1547-56. PMID:14656439
Page seeded by OCA on Sun Mar 30 22:56:59 2008
