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2jsx

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(New page: 200px<br /><applet load="2jsx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jsx" /> '''Solution structure of the E. coli Tat proofr...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sargent, F.]]
[[Category: Sargent, F.]]
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[[Category: Spronk, C.A.E.M.]]
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[[Category: Spronk, C A.E M.]]
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[[Category: Vuister, G.W.]]
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[[Category: Vuister, G W.]]
[[Category: chaperone]]
[[Category: chaperone]]
[[Category: cytoplasm]]
[[Category: cytoplasm]]
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[[Category: tat]]
[[Category: tat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:49:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:05:41 2008''

Revision as of 16:05, 21 February 2008

Image:2jsx.jpg

2jsx

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

2JSX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural diversity in twin-arginine signal peptide-binding proteins., Maillard J, Spronk CA, Buchanan G, Lyall V, Richardson DJ, Palmer T, Vuister GW, Sargent F, Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15641-6. Epub 2007 Sep 27. PMID:17901208

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