1w2b
From Proteopedia
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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 ... [(full description)]
About this Structure
1W2B is a [Protein complex] structure of sequences from [Escherichia coli] and [Haloarcula marismortui] with MG, NA, K, CL and CD as [ligands]. Structure known Active Site: AC1. 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 Tue Oct 30 16:22:37 2007
Categories: Escherichia coli | Haloarcula marismortui | Protein complex | Ban, N. | Bukau, B. | Deuerling, E. | Ferbitz, L. | Maier, T. | Patzelt, H. | CD | CL | K | MG | NA | Chaperone | Cotranslational folding | Nascent chain | Ribosomal protein | Ribosome | Ribosome associated factors | Rna-binding
