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1geg

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{{Seed}}
 
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[[Image:1geg.png|left|200px]]
 
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==CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE==
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The line below this paragraph, containing "STRUCTURE_1geg", creates the "Structure Box" on the page.
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<StructureSection load='1geg' size='340' side='right'caption='[[1geg]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1geg]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GEG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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{{STRUCTURE_1geg| PDB=1geg | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1geg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geg OCA], [https://pdbe.org/1geg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1geg RCSB], [https://www.ebi.ac.uk/pdbsum/1geg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1geg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BUDC_KLEPN BUDC_KLEPN] Catalyzes the reversible reduction of (S)-acetoin to 2,3-butanediol in the presence of NADH.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/1geg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1geg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of a ternary complex of meso-2,3-butanediol dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has been determined at 1.7 A resolution by means of molecular replacement and refined to a final R-factor of 0.194. The overall structure is similar to those of the other short chain dehydrogenase/reductase enzymes. The NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. The crystal structure revealed that mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase. Two residues around the active site, Gln140 and Gly183, forming hydrogen bonds with the inhibitor, are important but not sufficient for distinguishing stereoisomerism of a chiral substrate.
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===CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE===
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Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms.,Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M J Biochem. 2001 Feb;129(2):205-8. PMID:11173520<ref>PMID:11173520</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11173520}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1geg" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11173520 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11173520}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1GEG is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEG OCA].
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==Reference==
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<ref group="xtra">PMID:11173520</ref><references group="xtra"/>
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[[Category: Acetoin dehydrogenase]]
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[[Category: Klebsiella pneumoniae]]
[[Category: Klebsiella pneumoniae]]
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[[Category: Kurisu, G.]]
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[[Category: Large Structures]]
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[[Category: Kusunoki, M.]]
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[[Category: Kurisu G]]
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[[Category: Otagiri, M.]]
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[[Category: Kusunoki M]]
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[[Category: Ui, S.]]
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[[Category: Otagiri M]]
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[[Category: Sdr family]]
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[[Category: Ui S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:31:34 2009''
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Current revision

CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE

PDB ID 1geg

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