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| ==Structure of Glycerol-3-Phosphate Dehydrogenase, GPD1, from Sacharomyces Cerevisiae== | | ==Structure of Glycerol-3-Phosphate Dehydrogenase, GPD1, from Sacharomyces Cerevisiae== |
| <StructureSection load='4fgw' size='340' side='right' caption='[[4fgw]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4fgw' size='340' side='right'caption='[[4fgw]], [[Resolution|resolution]] 2.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4fgw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FGW FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4fgw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGW FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GPD1, DAR1, HOR1, OSG1, YDL022W, D2830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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]] 2.45Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerol-3-phosphate_dehydrogenase_(NAD(+)) Glycerol-3-phosphate dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.8 1.1.1.8] </span></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=4fgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgw OCA], [https://pdbe.org/4fgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fgw RCSB], [https://www.ebi.ac.uk/pdbsum/4fgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgw ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fgw RCSB], [http://www.ebi.ac.uk/pdbsum/4fgw PDBsum]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/GPD1_YEAST GPD1_YEAST]] Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.<ref>PMID:8196651</ref> | | [https://www.uniprot.org/uniprot/GPD1_YEAST GPD1_YEAST] Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.<ref>PMID:8196651</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism and provides Saccharomyces cerevisiae with protection against osmotic and anoxic stress. The first structure of a glycerol-3-phosphate dehydrogenase from S. cerevisiae, GPD1, is reported at 2.45 A resolution. The asymmetric unit contains two monomers, each of which is organized with N- and C-terminal domains. The N-terminal domain contains a classic Rossmann fold with the (beta-alpha-beta-alpha-beta)2 motif typical of many NAD+-dependent enzymes, while the C-terminal domain is mainly alpha-helical. Structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases and reveal that the Clostridium acetobutylican protein with PDB code 3ce9 is a glycerol-1-phosphate dehydrogenase.
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| Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 A resolution.,Alarcon DA, Nandi M, Carpena X, Fita I, Loewen PC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1279-83., doi: 10.1107/S1744309112037736. Epub 2012 Oct 26. PMID:23143232<ref>PMID:23143232</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Glycerol-3-Phosphate Dehydrogenase|Glycerol-3-Phosphate Dehydrogenase]] | | *[[Glycerol-3-phosphate dehydrogenase 3D structures|Glycerol-3-phosphate dehydrogenase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Saccharomyces cerevisiae s288c]] | | [[Category: Large Structures]] |
| [[Category: Aparicio, D]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Carpena, X]] | | [[Category: Aparicio D]] |
| [[Category: Fita, I]] | | [[Category: Carpena X]] |
| [[Category: Loewen, P]] | | [[Category: Fita I]] |
| [[Category: Munmun, N]] | | [[Category: Loewen P]] |
| [[Category: Dehydrogenase]]
| | [[Category: Munmun N]] |
| [[Category: Nad+]]
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| [[Category: Oxidoreductase]]
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