1x0v

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{{STRUCTURE_1x0v| PDB=1x0v | SCENE= }}
 
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===Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1===
 
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{{ABSTRACT_PUBMED_16460752}}
 
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==Disease==
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==Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1==
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[[http://www.uniprot.org/uniprot/GPDA_HUMAN GPDA_HUMAN]] Defects in GPD1 are a cause of hypertriglyceridemia, transient infantile (HTGTI) [MIM:[http://omim.org/entry/614480 614480]]. An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis.<ref>PMID:22226083</ref>
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<StructureSection load='1x0v' size='340' side='right'caption='[[1x0v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1x0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X0V FirstGlance]. <br>
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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]] 2.3&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1x0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x0v OCA], [https://pdbe.org/1x0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x0v RCSB], [https://www.ebi.ac.uk/pdbsum/1x0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x0v ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/GPDA_HUMAN GPDA_HUMAN] Defects in GPD1 are a cause of hypertriglyceridemia, transient infantile (HTGTI) [MIM:[https://omim.org/entry/614480 614480]. An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis.<ref>PMID:22226083</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/GPDA_HUMAN GPDA_HUMAN]
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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/x0/1x0v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1x0v 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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Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase 1 (GPD1) catalyzes the reversible biological conversion of dihydroxyacetone (DHAP) to glycerol-3-phosphate. The GPD1 protein was expressed in Escherichia coli, and purified as a fusion protein with glutathione S-transferase. Here we report the apoenzyme structure of GPD1 determined by multiwavelength anomalous diffraction phasing, and other complex structures with small molecules (NAD+ and DHAP) by the molecular replacement method. This enzyme structure is organized into two distinct domains, the N-terminal eight-stranded beta-sheet sandwich domain and the C-terminal helical substrate-binding domain. An electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analyses. In addition, the inhibitory effects of zinc and sulfate on GPDHs are assayed and discussed.
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==About this Structure==
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Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1).,Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z J Mol Biol. 2006 Mar 31;357(3):858-69. Epub 2006 Jan 18. PMID:16460752<ref>PMID:16460752</ref>
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[[1x0v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X0V OCA].
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==See Also==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Glycerol-3-Phosphate Dehydrogenase|Glycerol-3-Phosphate Dehydrogenase]]
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</div>
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<div class="pdbe-citations 1x0v" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:016460752</ref><references group="xtra"/><references/>
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*[[Glycerol-3-phosphate dehydrogenase 3D structures|Glycerol-3-phosphate dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ou, X.]]
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[[Category: Large Structures]]
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[[Category: Rao, Z.]]
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[[Category: Ou X]]
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[[Category: Gxgxxg motif]]
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[[Category: Rao Z]]
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[[Category: Oxidoreductase]]
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[[Category: Two independent domain]]
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Current revision

Crystal Structure of Homo Sapien Glycerol-3-Phosphate Dehydrogenase 1

PDB ID 1x0v

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