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1w2b

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[[Image:1w2b.gif|left|200px]]
[[Image:1w2b.gif|left|200px]]
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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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The line below this paragraph, containing "STRUCTURE_1w2b", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+0'>AC1</scene>
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{{STRUCTURE_1w2b| PDB=1w2b | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2b OCA], [http://www.ebi.ac.uk/pdbsum/1w2b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w2b RCSB]</span>
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'''TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S'''
'''TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S'''
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[[Category: Maier, T.]]
[[Category: Maier, T.]]
[[Category: Patzelt, H.]]
[[Category: Patzelt, H.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: cotranslational folding]]
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[[Category: Cotranslational folding]]
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[[Category: nascent chain]]
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[[Category: Nascent chain]]
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[[Category: ribosomal protein]]
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[[Category: Ribosomal protein]]
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[[Category: ribosome]]
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[[Category: Ribosome]]
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[[Category: ribosome_associated factor]]
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[[Category: Ribosome_associated factor]]
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[[Category: rna-binding]]
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[[Category: Rna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:03:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:09 2008''
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Revision as of 10:03, 3 May 2008

Image:1w2b.gif

Template:STRUCTURE 1w2b

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 Page seeded by OCA on Sat May 3 13:03:22 2008

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