1w2b

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[[Image:1w2b.gif|left|200px]]<br /><applet load="1w2b" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w2b.gif|left|200px]]
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caption="1w2b, resolution 3.50&Aring;" />
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'''TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S'''<br />
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{{Structure
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|PDB= 1w2b |SIZE=350|CAPTION= <scene name='initialview01'>1w2b</scene>, resolution 3.50&Aring;
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+0'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=CD:CADMIUM ION'>CD</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W2B is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+0'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2B OCA].
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1W2B is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2B OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15334087 15334087]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15334087 15334087]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
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[[Category: ribosomal protein]]
[[Category: ribosomal protein]]
[[Category: ribosome]]
[[Category: ribosome]]
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[[Category: ribosome_associated factors]]
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[[Category: ribosome_associated factor]]
[[Category: rna-binding]]
[[Category: rna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:51:08 2008''

Revision as of 12:51, 20 March 2008

Image:1w2b.gif


PDB ID 1w2b

Drag the structure with the mouse to rotate
, resolution 3.50Å
Sites:
Ligands: , , , and
Coordinates: save as pdb, mmCIF, xml



TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S


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

1W2B is a Protein complex structure of sequences from Escherichia coli and Haloarcula marismortui. 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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