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<StructureSection load='3qvb' size='340' side='right'caption='[[3qvb]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='3qvb' size='340' side='right'caption='[[3qvb]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qvb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QVB FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qvb]] is a 1 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=3QVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QVB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 2.26&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3q4s|3q4s]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycogenin_glucosyltransferase Glycogenin glucosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.186 2.4.1.186] </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=3qvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qvb OCA], [https://pdbe.org/3qvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qvb RCSB], [https://www.ebi.ac.uk/pdbsum/3qvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qvb 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=3qvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qvb OCA], [https://pdbe.org/3qvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qvb RCSB], [https://www.ebi.ac.uk/pdbsum/3qvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qvb ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN]] Glycogen storage disease due to glycogenin deficiency. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN] Glycogen storage disease due to glycogenin deficiency. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN]] Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.  
[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN] Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycogenin initiates the synthesis of a maltosaccharide chain covalently attached to itself on Tyr195 via a stepwise glucosylation reaction, priming glycogen synthesis. We have captured crystallographic snapshots of human glycogenin during its reaction cycle, revealing a dynamic conformational switch between ground and active states mediated by the sugar donor UDP-glucose. This switch includes the ordering of a polypeptide stretch containing Tyr195, and major movement of an approximately 30-residue "lid" segment covering the active site. The rearranged lid guides the nascent maltosaccharide chain into the active site in either an intra- or intersubunit mode dependent upon chain length and steric factors and positions the donor and acceptor sugar groups for catalysis. The Thr83Met mutation, which causes glycogen storage disease XV, is conformationally locked in the ground state and catalytically inactive. Our data highlight the conformational plasticity of glycogenin and coexistence of two modes of glucosylation as integral to its catalytic mechanism.
 
Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis.,Chaikuad A, Froese DS, Berridge G, von Delft F, Oppermann U, Yue WW Proc Natl Acad Sci U S A. 2011 Dec 12. PMID:22160680<ref>PMID:22160680</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qvb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Glycogenin|Glycogenin]]
*[[Glycogenin|Glycogenin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glycogenin glucosyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Chaikuad, A]]
[[Category: Chaikuad A]]
[[Category: Delft, F von]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Froese DS]]
[[Category: Froese, D S]]
[[Category: Krysztofinska E]]
[[Category: Krysztofinska, E]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Weigelt J]]
[[Category: Structural genomic]]
[[Category: Yue WW]]
[[Category: Weigelt, J]]
[[Category: Von Delft F]]
[[Category: Yue, W W]]
[[Category: Glycogen biosynthesis]]
[[Category: Glycosylation]]
[[Category: Glycosyltransferase]]
[[Category: Transferase]]

Latest revision as of 12:00, 14 March 2024

Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP

3qvb, resolution 2.26Å

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