1nxu: Difference between revisions

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[[Image:1nxu.gif|left|200px]]<br /><applet load="1nxu" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nxu.gif|left|200px]]
caption="1nxu, resolution 1.80&Aring;" />
 
'''CRYSTAL STRUCTURE OF E. COLI HYPOTHETICAL OXIDOREDUCTASE YIAK NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER82.'''<br />
{{Structure
|PDB= 1nxu |SIZE=350|CAPTION= <scene name='initialview01'>1nxu</scene>, resolution 1.80&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY=
|GENE= YIAK OR B3575 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''CRYSTAL STRUCTURE OF E. COLI HYPOTHETICAL OXIDOREDUCTASE YIAK NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER82.'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1NXU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXU OCA].  
1NXU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXU OCA].  


==Reference==
==Reference==
A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)., Forouhar F, Lee I, Benach J, Kulkarni K, Xiao R, Acton TB, Montelione GT, Tong L, J Biol Chem. 2004 Mar 26;279(13):13148-55. Epub 2004 Jan 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14718529 14718529]
A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)., Forouhar F, Lee I, Benach J, Kulkarni K, Xiao R, Acton TB, Montelione GT, Tong L, J Biol Chem. 2004 Mar 26;279(13):13148-55. Epub 2004 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14718529 14718529]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
[[Category: structural genomics]]
[[Category: structural genomic]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:03:05 2008''

Revision as of 11:03, 20 March 2008

File:1nxu.gif


Drag the structure with the mouse to rotate
1nxu, resolution 1.80Å
Ligands: SO4
Gene: YIAK OR B3575 (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF E. COLI HYPOTHETICAL OXIDOREDUCTASE YIAK NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER82.


Overview

Escherichia coli YiaK catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH. It belongs to a large family of oxidoreductases that is conserved in archaea, bacteria, and eukaryotes but shows no sequence homology to other proteins. We report here the crystal structures at up to 2.0-A resolution of YiaK alone and in complex with NAD-tartrate. YiaK has a new polypeptide backbone fold and a novel mode of recognizing the NAD cofactor. In addition, NAD is bound in an unusual conformation, at the interface of a dimer of the enzyme. The crystallographic analysis unexpectedly revealed the binding of tartrate in the active site. Enzyme kinetics studies confirm that tartrate and the related D-malate are inhibitors of YiaK. In contrast to most other enzymes where substrate binding produces a more closed conformation, the binding of NAD-tartrate to YiaK produces a more open active site. The free enzyme conformation is incompatible with NAD binding. His(44) is likely the catalytic residue of the enzyme.

About this Structure

1NXU is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK)., Forouhar F, Lee I, Benach J, Kulkarni K, Xiao R, Acton TB, Montelione GT, Tong L, J Biol Chem. 2004 Mar 26;279(13):13148-55. Epub 2004 Jan 12. PMID:14718529

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