2N62

ddFLN5+110

Summary for 2N62

• Entry DOI: 10.2210/pdb2n62/pdb
• NMR Information: BMRB: 25748
• Descriptor: gelation factor, secretion monitor chimera (1 entity in total)
• Functional Keywords: translation
• Biological source: Dictyostelium discoideum, Escherichia coli (slime mold)
• Cellular location: Cytoplasm, cytosol : P62395
• Total number of polymer chains: 1
• Total formula weight: 23420.72

Authors

Cabrita, L.D.,Cassaignau, A.M.E.,Launay, H.M.M.,Waudby, C.A.,Camilloni, C.,Robertson, A.L.,Wang, X.,Wlodarski, T.,Wentink, A.S.,Vendruscolo, M.,Dobson, C.M.,Christodoulou, J. (deposition date: 2015-08-10, release date: 2016-03-02, Last modification date: 2024-05-01)

Primary citation

Cabrita, L.D.,Cassaignau, A.M.,Launay, H.M.,Waudby, C.A.,Wlodarski, T.,Camilloni, C.,Karyadi, M.E.,Robertson, A.L.,Wang, X.,Wentink, A.S.,Goodsell, L.S.,Woolhead, C.A.,Vendruscolo, M.,Dobson, C.M.,Christodoulou, J.
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.
Nat.Struct.Mol.Biol., 23:278-285, 2016

PubMed Abstract: Although detailed pictures of ribosome structures are emerging, little is known about the structural and cotranslational folding properties of nascent polypeptide chains at the atomic level. Here we used solution-state NMR spectroscopy to define a structural ensemble of a ribosome-nascent chain complex (RNC) formed during protein biosynthesis in Escherichia coli, in which a pair of immunoglobulin-like domains adopts a folded N-terminal domain (FLN5) and a disordered but compact C-terminal domain (FLN6). To study how FLN5 acquires its native structure cotranslationally, we progressively shortened the RNC constructs. We found that the ribosome modulates the folding process, because the complete sequence of FLN5 emerged well beyond the tunnel before acquiring native structure, whereas FLN5 in isolation folded spontaneously, even when truncated. This finding suggests that regulating structure acquisition during biosynthesis can reduce the probability of misfolding, particularly of homologous domains.

PubMed: 26926436
DOI: 10.1038/nsmb.3182

Experimental method

SOLUTION NMR