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| {{STRUCTURE_1w2b| PDB=1w2b | SCENE= }} | | {{STRUCTURE_1w2b| PDB=1w2b | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15334087}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15334087 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15334087}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ribosome_associated factor]] | | [[Category: Ribosome_associated factor]] |
| [[Category: Rna-binding]] | | [[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 Mon Jul 28 04:15:15 2008'' |
