1oms
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(New page: 200px<br /><applet load="1oms" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oms, resolution 2.30Å" /> '''Structure determinat...)
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Revision as of 20:53, 20 November 2007
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Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.
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
1OMS is a Single protein structure of sequence from Escherichia coli with SO4, PG4, SO2 and GOL as ligands. 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
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