2jsx

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[[Image:2jsx.jpg|left|200px]]
[[Image:2jsx.jpg|left|200px]]
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{{Structure
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|PDB= 2jsx |SIZE=350|CAPTION= <scene name='initialview01'>2jsx</scene>
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The line below this paragraph, containing "STRUCTURE_2jsx", creates the "Structure Box" on the page.
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|SITE=
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|GENE= napD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2jsx| PDB=2jsx | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsx OCA], [http://www.ebi.ac.uk/pdbsum/2jsx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jsx RCSB]</span>
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'''Solution structure of the E. coli Tat proofreading chaperone protein NapD'''
'''Solution structure of the E. coli Tat proofreading chaperone protein NapD'''
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[[Category: Spronk, C A.E M.]]
[[Category: Spronk, C A.E M.]]
[[Category: Vuister, G W.]]
[[Category: Vuister, G W.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: cytoplasm]]
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[[Category: Cytoplasm]]
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[[Category: napd]]
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[[Category: Napd]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: proofreading]]
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[[Category: Proofreading]]
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[[Category: protein]]
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[[Category: Protein]]
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[[Category: tat]]
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[[Category: Tat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:15:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:01:22 2008''
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Revision as of 06:15, 4 May 2008

Image:2jsx.jpg

Template:STRUCTURE 2jsx

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 Page seeded by OCA on Sun May 4 09:15:53 2008

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