4fgw

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== Structural highlights ==
== Structural highlights ==
<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>
<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>
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</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>
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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]] 2.45&#8491;</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=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>
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</table>
== Function ==
== Function ==
[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>
[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>
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<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4fgw" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==

Current revision

Structure of Glycerol-3-Phosphate Dehydrogenase, GPD1, from Sacharomyces Cerevisiae

PDB ID 4fgw

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Proteopedia Page Contributors and Editors (what is this?)

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