2N62

ddFLN5+110

2N62 の概要

• エントリーDOI: 10.2210/pdb2n62/pdb
• NMR情報: BMRB: 25748
• 分子名称: gelation factor, secretion monitor chimera (1 entity in total)
• 機能のキーワード: translation
• 由来する生物種: Dictyostelium discoideum, Escherichia coli (slime mold)
• 細胞内の位置: Cytoplasm, cytosol : P62395
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23420.72

構造登録者

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. (登録日: 2015-08-10, 公開日: 2016-03-02, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

SOLUTION NMR