8cvx
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8cvx]] is a 8 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=8CVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CVX FirstGlance]. <br> | <table><tr><td colspan='2'>[[8cvx]] is a 8 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=8CVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CVX FirstGlance]. <br> | ||
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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></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=8cvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cvx OCA], [https://pdbe.org/8cvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cvx RCSB], [https://www.ebi.ac.uk/pdbsum/8cvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cvx ProSAT]</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=8cvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cvx OCA], [https://pdbe.org/8cvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cvx RCSB], [https://www.ebi.ac.uk/pdbsum/8cvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cvx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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[https://www.uniprot.org/uniprot/GYS1_HUMAN GYS1_HUMAN] Glycogen storage disease due to muscle and heart glycogen synthase deficiency. The disease is caused by variants affecting the gene represented in this entry. | [https://www.uniprot.org/uniprot/GYS1_HUMAN GYS1_HUMAN] Glycogen storage disease due to muscle and heart glycogen synthase deficiency. The disease is caused by variants affecting the gene represented in this entry. | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/GYS1_HUMAN GYS1_HUMAN] | + | [https://www.uniprot.org/uniprot/GYS1_HUMAN GYS1_HUMAN] Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.<ref>PMID:35835870</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glycogen is the primary energy reserve in mammals, and dysregulation of glycogen metabolism can result in glycogen storage diseases (GSDs). In muscle, glycogen synthesis is initiated by the enzymes glycogenin-1 (GYG1), which seeds the molecule by autoglucosylation, and glycogen synthase-1 (GYS1), which extends the glycogen chain. Although both enzymes are required for proper glycogen production, the nature of their interaction has been enigmatic. Here, we present the human GYS1:GYG1 complex in multiple conformations representing different functional states. We observe an asymmetric conformation of GYS1 that exposes an interface for close GYG1 association, and propose this state facilitates handoff of the GYG1-associated glycogen chain to a GYS1 subunit for elongation. Full activation of GYS1 widens the GYG1-binding groove, enabling GYG1 release concomitant with glycogen chain growth. This structural mechanism connecting chain nucleation and extension explains the apparent stepwise nature of glycogen synthesis and suggests distinct states to target for GSD-modifying therapeutics. | ||
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| + | The structural mechanism of human glycogen synthesis by the GYS1-GYG1 complex.,Fastman NM, Liu Y, Ramanan V, Merritt H, Ambing E, DePaoli-Roach AA, Roach PJ, Hurley TD, Mellem KT, Ullman JC, Green E, Morgans D Jr, Tzitzilonis C Cell Rep. 2022 Jul 5;40(1):111041. doi: 10.1016/j.celrep.2022.111041. PMID:35793618<ref>PMID:35793618</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8cvx" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Glycogenin|Glycogenin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Human glycogenin-1 and glycogen synthase-1 complex in the presence of glucose-6-phosphate
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