2JSX

Solution structure of the E. coli Tat proofreading chaperone protein NapD

2JSX の概要

• エントリーDOI: 10.2210/pdb2jsx/pdb
• NMR情報: BMRB: 15381
• 分子名称: Protein napD (1 entity in total)
• 機能のキーワード: napd, tat, proofreading, protein, cytoplasm, chaperone
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10546.59

構造登録者

Spronk, C.A.E.M.,Vuister, G.W.,Sargent, F. (登録日: 2007-07-17, 公開日: 2007-08-21, 最終更新日: 2024-05-08)

主引用文献

Maillard, J.,Spronk, C.A.E.M.,Buchanan, G.,Lyall, V.,Richardson, D.J.,Palmer, T.,Vuister, G.W.,Sargent, F.
Structural diversity in twin-arginine signal peptide-binding proteins.
Proc.Natl.Acad.Sci.Usa, 104:15641-15646, 2007

PubMed Abstract: The twin-arginine transport (Tat) system is dedicated to the translocation of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat system by signal peptides containing a twin-arginine motif. In Escherichia coli, many Tat substrates bind redox-active cofactors in the cytoplasm before transport. Coordination of cofactor insertion with protein export involves a "Tat proofreading" process in which chaperones bind twin-arginine signal peptides, thus preventing premature export. The initial Tat signal-binding proteins described belonged to the TorD family, which are required for assembly of N- and S-oxide reductases. Here, we report that E. coli NapD is a Tat signal peptide-binding chaperone involved in biosynthesis of the Tat-dependent nitrate reductase NapA. NapD binds tightly and specifically to the NapA twin-arginine signal peptide and suppresses signal peptide translocation activity such that transport via the Tat pathway is retarded. High-resolution, heteronuclear, multidimensional NMR spectroscopy reveals the 3D solution structure of NapD. The chaperone adopts a ferredoxin-type fold, which is completely distinct from the TorD family. Thus, NapD represents a new family of twin-arginine signal-peptide-binding proteins.

PubMed: 17901208
DOI: 10.1073/pnas.0703967104

実験手法

SOLUTION NMR