3a28: Difference between revisions

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-[[Image:3a28.png|left|200px]]
-{{STRUCTURE_3a28|  PDB=3a28  |  SCENE=  }}
+==Crystal structure of L-2,3-butanediol dehydrogenase==
+<StructureSection load='3a28' size='340' side='right'caption='[[3a28]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3a28]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A28 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=3a28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a28 OCA], [https://pdbe.org/3a28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a28 RCSB], [https://www.ebi.ac.uk/pdbsum/3a28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a28 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BUDC_CORGT BUDC_CORGT] Catalyzes the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol (L-BD) in the presence of NADH. To a lesser extent, can also catalyze the irreversible reduction of diacetyl to (S)-acetoin. Cannot oxidize meso-BD, D-BD, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, and n-propanol. Cannot reduce (R)-acetoin, acetol, dihydroxyacetone and 2,4-pentanedione.[REFERENCE:1]<ref>PMID:11577733</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a2/3a28_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3a28 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+,3-butanediol dehydrogenase (BDH) catalyzes the NAD-dependent redox reaction between acetoin and 2,3-butanediol. There are three types of homologous BDH, each stereospecific for both substrate and product. To establish how these homologous enzymes possess differential stereospecificities, we determined the crystal structure of l-BDH with a bound inhibitor at 2.0 A. Comparison with the inhibitor binding mode of meso-BDH highlights the role of a hydrogen-bond from a conserved Trp residue(192). Site-directed mutagenesis of three active site residues of meso-BDH, including Trp(190), which corresponds to Trp(192) of L-BDH, converted its stereospecificity to that of L-BDH. This result confirms the importance of conserved residues in modifying the stereospecificity of homologous enzymes.
-===Crystal structure of L-2,3-butanediol dehydrogenase===
+Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases.,Otagiri M, Ui S, Takusagawa Y, Ohtsuki T, Kurisu G, Kusunoki M FEBS Lett. 2010 Jan 4;584(1):219-23. Epub . PMID:19941855<ref>PMID:19941855</ref>
-{{ABSTRACT_PUBMED_19941855}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 3a28" style="background-color:#fffaf0;"></div>
-[[3a28]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A28 OCA].
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:019941855</ref><references group="xtra"/>
+</StructureSection>
 [[Category: Corynebacterium glutamicum]]
-[[Category: Kurisu, G.]]
+[[Category: Large Structures]]
-[[Category: Kusunoki, M.]]
+[[Category: Kurisu G]]
-[[Category: Otagiri, M.]]
+[[Category: Kusunoki M]]
-[[Category: Ui, S.]]
+[[Category: Otagiri M]]
-[[Category: Chiral substrate recognition]]
+[[Category: Ui S]]
-[[Category: Oxidoreductase]]