1p9y
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1p9y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9y, resolution 2.15Å" /> '''Ribosome binding of ...)
Next diff →
Revision as of 21:30, 20 November 2007
|
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 with ACY as ligand. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 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 Tue Nov 20 23:37:25 2007
