1p9y
From Proteopedia
(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 ...) |
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| - | [[Image:1p9y.gif|left|200px]]<br /><applet load="1p9y" size=" | + | [[Image:1p9y.gif|left|200px]]<br /><applet load="1p9y" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p9y, resolution 2.15Å" /> | caption="1p9y, resolution 2.15Å" /> | ||
'''Ribosome binding of E. coli Trigger Factor mutant F44L.'''<br /> | '''Ribosome binding of E. coli Trigger Factor mutant F44L.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The exit tunnel region of the ribosome is well established as a focal | + | 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== | ==About this Structure== | ||
| - | 1P9Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http:// | + | 1P9Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:46 2008'' |
Revision as of 12:26, 21 February 2008
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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 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
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