1w26: Difference between revisions

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[[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1w26, resolution 2.70Å" />

'''TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1W26 OCA].

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==

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[[Category: ribosome associated protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 05:12:~~12 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1w26, resolution 2.70&Aring;" />
 '''TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS'''<br />
 ==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.
+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==
-W26 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W26 OCA].
+W26 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==
@@ Line 26: / Line 26: @@
 [[Category: ribosome associated protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:12:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:38 2008''