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| | ==Glucose1,2cyclic phosphate bound activated state of Yeast Glycogen Synthase== | | ==Glucose1,2cyclic phosphate bound activated state of Yeast Glycogen Synthase== |
| - | <StructureSection load='4kq2' size='340' side='right' caption='[[4kq2]], [[Resolution|resolution]] 2.95Å' scene=''> | + | <StructureSection load='4kq2' size='340' side='right'caption='[[4kq2]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kq2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KQ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kq2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_FostersO Saccharomyces cerevisiae FostersO]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KQ2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1S3:(2R,3AR,5R,6S,7S,7AR)-5-(HYDROXYMETHYL)TETRAHYDRO-3AH-[1,3,2]DIOXAPHOSPHOLO[4,5-B]PYRAN-2,6,7-TRIOL+2-OXIDE'>1S3</scene>, <scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1S3:(2R,3AR,5R,6S,7S,7AR)-5-(HYDROXYMETHYL)TETRAHYDRO-3AH-[1,3,2]DIOXAPHOSPHOLO[4,5-B]PYRAN-2,6,7-TRIOL+2-OXIDE'>1S3</scene>, <scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kq1|4kq1]], [[4kqm|4kqm]]</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=4kq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kq2 OCA], [https://pdbe.org/4kq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kq2 RCSB], [https://www.ebi.ac.uk/pdbsum/4kq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kq2 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FOSTERSO_3265, GSY2 YLR258W L8479.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=764101 Baker's yeast])</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=4kq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kq2 OCA], [http://pdbe.org/4kq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kq2 RCSB], [http://www.ebi.ac.uk/pdbsum/4kq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kq2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Chikwana, V M]] | + | [[Category: Saccharomyces cerevisiae FostersO]] |
| - | [[Category: Hurley, T D]] | + | [[Category: Chikwana VM]] |
| - | [[Category: Glucosylation]] | + | [[Category: Hurley TD]] |
| - | [[Category: Glucosyltransferase]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gt-b]]
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| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
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.
Publication Abstract from PubMed
Glycogen is a glucose polymer that contains minor amounts of covalently attached phosphate. Hyperphosphorylation is deleterious to glycogen structure and can lead to Lafora disease. Recently, it was demonstrated that glycogen synthase catalyzes glucose-phosphate transfer in addition to its characteristic glucose transfer reaction. Glucose-1,2-cyclic-phosphate (GCP) was proposed to be formed from UDP-Glc breakdown and subsequently transferred, thus providing a source of phosphate found in glycogen. To gain further insight into the molecular basis for glucose-phosphate transfer, two structures of yeast glycogen synthase were determined; a 3.0-A resolution structure of the complex with UMP/GCP and a 2.8-A resolution structure of the complex with UDP/glucose. Structural superposition of the complexes revealed that the bound ligands and most active site residues are positioned similarly, consistent with the use of a common transfer mechanism for both reactions. The N-terminal domain of the UDPglucose complex was found to be 13.3 degrees more closed compared with a UDP complex. However, the UMPGCP complex was 4.8 degrees less closed than the glucose complex, which may explain the low efficiency of GCP transfer. Modeling of either alpha- or beta-glucose or a mixture of both anomers can account for the observed electron density of the UDPglucose complex. NMR studies of UDP-Glc hydrolysis by yeast glycogen synthase were used to verify the stereochemistry of the product, and they also showed synchronous GCP accumulation. The similarities in the active sites of glycogen synthase and glycogen phosphorylase support the idea of a common catalytic mechanism in GT-B enzymes independent of the specific reaction catalyzed.
Structural basis for 2'-phosphate incorporation into glycogen by glycogen synthase.,Chikwana VM, Khanna M, Baskaran S, Tagliabracci VS, Contreras CJ, Depaoli-Roach A, Roach PJ, Hurley TD Proc Natl Acad Sci U S A. 2013 Dec 24;110(52):20976-81. doi:, 10.1073/pnas.1310106111. Epub 2013 Dec 9. PMID:24324135[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chikwana VM, Khanna M, Baskaran S, Tagliabracci VS, Contreras CJ, Depaoli-Roach A, Roach PJ, Hurley TD. Structural basis for 2'-phosphate incorporation into glycogen by glycogen synthase. Proc Natl Acad Sci U S A. 2013 Dec 24;110(52):20976-81. doi:, 10.1073/pnas.1310106111. Epub 2013 Dec 9. PMID:24324135 doi:http://dx.doi.org/10.1073/pnas.1310106111
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