1w2b
From Proteopedia
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[[Image:1w2b.gif|left|200px]] | [[Image:1w2b.gif|left|200px]] | ||
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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.]] | ||
- | [[Category: | + | [[Category: Chaperone]] |
- | [[Category: | + | [[Category: Cotranslational folding]] |
- | [[Category: | + | [[Category: Nascent chain]] |
- | [[Category: | + | [[Category: Ribosomal protein]] |
- | [[Category: | + | [[Category: Ribosome]] |
- | [[Category: | + | [[Category: Ribosome_associated factor]] |
- | [[Category: | + | [[Category: Rna-binding]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:03:22 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 10:03, 3 May 2008
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