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| | ==Maltodextarn bound activated state form of yeast glycogen synthase isoform 2== | | ==Maltodextarn bound activated state form of yeast glycogen synthase isoform 2== |
| - | <StructureSection load='3rt1' size='340' side='right' caption='[[3rt1]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3rt1' size='340' side='right'caption='[[3rt1]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rt1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RT1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RT1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rt1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RT1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nb0|3nb0]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=PRD_900030:alpha-maltopentaose'>PRD_900030</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSY2, L8479.8, YLR258W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3rt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rt1 OCA], [https://pdbe.org/3rt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rt1 RCSB], [https://www.ebi.ac.uk/pdbsum/3rt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rt1 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycogen(starch)_synthase Glycogen(starch) synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.11 2.4.1.11] </span></td></tr>
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| - | <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=3rt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rt1 OCA], [http://pdbe.org/3rt1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rt1 RCSB], [http://www.ebi.ac.uk/pdbsum/3rt1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rt1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GYS2_YEAST GYS2_YEAST]] Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen. | + | [https://www.uniprot.org/uniprot/GYS2_YEAST GYS2_YEAST] Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Glycogen synthase is a rate-limiting enzyme in the biosynthesis of glycogen and has an essential role in glucose homeostasis. The three-dimensional structures of yeast glycogen synthase (Gsy2p) complexed with maltooctaose identified four conserved maltodextrin-binding sites distributed across the surface of the enzyme. Site-1 is positioned on the N-terminal domain, site-2 and site-3 are present on the C-terminal domain, and site-4 is located in an interdomain cleft adjacent to the active site. Mutation of these surface sites decreased glycogen binding and catalytic efficiency toward glycogen. Mutations within site-1 and site-2 reduced the V(max)/S(0.5) for glycogen by 40- and 70-fold, respectively. Combined mutation of site-1 and site-2 decreased the V(max)/S(0.5) for glycogen by >3000-fold. Consistent with the in vitro data, glycogen accumulation in glycogen synthase-deficient yeast cells (Deltagsy1-gsy2) transformed with the site-1, site-2, combined site-1/site-2, or site-4 mutant form of Gsy2p was decreased by up to 40-fold. In contrast to the glycogen results, the ability to utilize maltooctaose as an in vitro substrate was unaffected in the site-2 mutant, moderately affected in the site-1 mutant, and almost completely abolished in the site-4 mutant. These data show that the ability to utilize maltooctaose as a substrate can be independent of the ability to utilize glycogen. Our data support the hypothesis that site-1 and site-2 provide a "toehold mechanism," keeping glycogen synthase tightly associated with the glycogen particle, whereas site-4 is more closely associated with positioning of the nonreducing end during catalysis.
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| - | Multiple Glycogen-binding Sites in Eukaryotic Glycogen Synthase Are Required for High Catalytic Efficiency toward Glycogen.,Baskaran S, Chikwana VM, Contreras CJ, Davis KD, Wilson WA, Depaoli-Roach AA, Roach PJ, Hurley TD J Biol Chem. 2011 Sep 30;286(39):33999-4006. Epub 2011 Aug 11. PMID:21835915<ref>PMID:21835915</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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| - | <div class="pdbe-citations 3rt1" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Baskaran, S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hurley, T D]] | + | [[Category: Baskaran S]] |
| - | [[Category: Glycogen binding]] | + | [[Category: Hurley TD]] |
| - | [[Category: Glycosyl transferase]]
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| - | [[Category: Maltodextarn binding]]
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| - | [[Category: Rossmann fold]]
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| - | [[Category: Transferase]]
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