3a28
From Proteopedia
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| - | {{STRUCTURE_3a28| PDB=3a28 | SCENE= }} | ||
| - | ===Crystal structure of L-2,3-butanediol dehydrogenase=== | ||
| - | {{ABSTRACT_PUBMED_19941855}} | ||
| - | == | + | ==Crystal structure of L-2,3-butanediol dehydrogenase== |
| - | [[http://www.uniprot.org/uniprot/BUDC_CORGT BUDC_CORGT | + | <StructureSection load='3a28' size='340' side='right'caption='[[3a28]], [[Resolution|resolution]] 2.00Å' 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]] 2Å</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 == | ||
| + | 2,3-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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 3a28" style="background-color:#fffaf0;"></div> |
| - | [[Category: Kurisu | + | == References == |
| - | [[Category: Kusunoki | + | <references/> |
| - | [[Category: Otagiri | + | __TOC__ |
| - | [[Category: Ui | + | </StructureSection> |
| - | + | [[Category: Corynebacterium glutamicum]] | |
| - | + | [[Category: Large Structures]] | |
| + | [[Category: Kurisu G]] | ||
| + | [[Category: Kusunoki M]] | ||
| + | [[Category: Otagiri M]] | ||
| + | [[Category: Ui S]] | ||
Current revision
Crystal structure of L-2,3-butanediol dehydrogenase
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