1w2b
|
TRIGGER FACTOR RIBOSOME BINDING DOMAIN IN COMPLEX WITH 50S
OverviewOverview
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 StructureAbout 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. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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 Dec 18 18:27:12 2007