2wsb: Difference between revisions

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 <StructureSection load='2wsb' size='340' side='right'caption='[[2wsb]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wsb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WSB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wsb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WSB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POL:N-PROPANOL'>POL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Galactitol_2-dehydrogenase Galactitol 2-dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.16 1.1.1.16] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=POL:N-PROPANOL'>POL</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wsb OCA], [https://pdbe.org/2wsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wsb RCSB], [https://www.ebi.ac.uk/pdbsum/2wsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wsb ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GATDH_CERSP GATDH_CERSP] Catalyzes the interconversion of galactitol to the rare sugar L-tagatose (PubMed:7551050). Shows activity with a wide range of substrates, and catalyzes the oxidation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols (PubMed:7551050, PubMed:15296184). Shows high activity with D-threitol, xylitol, 1,2-hexanediol, 1,2-pentanediol, 2-hexanol, L-erythrulose, D-ribulose and acetoin (PubMed:7551050). Specific for NAD(+) (PubMed:7551050).<ref>PMID:15296184</ref> <ref>PMID:7551050</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wsb ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Galactitol 2-dehydrogenase (GatDH) belongs to the protein superfamily of short-chain dehydrogenases. As an enzyme capable of the stereo- and regioselective modification of carbohydrates, it exhibits a high potential for application in biotechnology as a biocatalyst. We have determined the crystal structure of the binary form of GatDH in complex with its cofactor NAD(H) and of the ternary form in complex with NAD(H) and three different substrates. The active form of GatDH constitutes a homo-tetramer with two magnesium-ion binding sites each formed by two opposing C termini. The catalytic tetrad is formed by Asn(116), Ser(144), Tyr(159), and Lys(163). GatDH structurally aligns well with related members of the short-chain dehydrogenase family. The substrate binding pocket can be divided into two parts of different size and polarity. In the smaller part, the side chains of amino acids Ser(144), Ser(146), and Asn(151) are important determinants for the binding specificity and the orientation of (pro-) chiral compounds. The larger part of the pocket is elongated and flanked by polar and non-polar residues, enabling a rather broad substrate spectrum. The presented structures provide valuable information for a rational design of this enzyme to improve its stability against pH, temperature, or solvent concentration and to optimize product yield in bioreactors.
-Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D.,Carius Y, Christian H, Faust A, Zander U, Klink BU, Kornberger P, Kohring GW, Giffhorn F, Scheidig AJ J Biol Chem. 2010 Jun 25;285(26):20006-14. Epub 2010 Apr 21. PMID:20410293<ref>PMID:20410293</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2wsb" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhodococcus capsulatus molisch 1907]]
+[[Category: Cereibacter sphaeroides]]
-[[Category: Galactitol 2-dehydrogenase]]
 [[Category: Large Structures]]
-[[Category: Carius, Y]]
+[[Category: Carius Y]]
-[[Category: Christian, H]]
+[[Category: Christian H]]
-[[Category: Faust, A]]
+[[Category: Faust A]]
-[[Category: Giffhorn, F]]
+[[Category: Giffhorn F]]
-[[Category: Kohring, G W]]
+[[Category: Kohring GW]]
-[[Category: Kornberger, P]]
+[[Category: Kornberger P]]
-[[Category: Scheidig, A J]]
+[[Category: Scheidig AJ]]
-[[Category: Oxidoreductase]]
-[[Category: Rossmann fold]]
-[[Category: Sdr]]
-[[Category: Tagatose]]