1w26
From Proteopedia
(New page: 200px<br /><applet load="1w26" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w26, resolution 2.70Å" /> '''TRIGGER FACTOR IN CO...) |
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| - | [[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size=" | + | [[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w26, resolution 2.70Å" /> | caption="1w26, resolution 2.70Å" /> | ||
'''TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS'''<br /> | '''TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During protein biosynthesis, nascent polypeptide chains that emerge from | + | During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we present a 2.7 A crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding 'tail', the peptidyl-prolyl isomerase 'head', the carboxy-terminal 'arms' and connecting regions building up the 'back'. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones. |
==About this Structure== | ==About this Structure== | ||
| - | 1W26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1W26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W26 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ribosome associated protein]] | [[Category: ribosome associated protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:38 2008'' |
Revision as of 13:39, 21 February 2008
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TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS
Overview
During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we present a 2.7 A crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding 'tail', the peptidyl-prolyl isomerase 'head', the carboxy-terminal 'arms' and connecting regions building up the 'back'. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones.
About this Structure
1W26 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins., Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N, Nature. 2004 Sep 30;431(7008):590-6. Epub 2004 Aug 29. PMID:15334087
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