1nxu

<table><tr><td colspan='2'>[[1nxu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NXU FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YIAK OR B3575 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxu OCA], [http://pdbe.org/1nxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nxu RCSB], [http://www.ebi.ac.uk/pdbsum/1nxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nxu ProSAT], [http://www.topsan.org/Proteins/NESGC/1nxu TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/DLGD_ECOLI DLGD_ECOLI]] Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate.<ref>PMID:11741871</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:14718529</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1nxu" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Acton, T B]]

[[Category: Benach, J]]

[[Category: Forouhar, F]]

[[Category: Kulkarni, K]]

[[Category: Lee, I]]

[[Category: Montelione, G T]]

[[Category: Structural genomic]]

[[Category: Rost, B]]

[[Category: Shastry, R]]

[[Category: Tong, L]]

[[Category: Xiao, R]]

[[Category: PSI, Protein structure initiative]]