3v8y: Difference between revisions

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==Structure of apo-glycogenin truncated at residue 270==
==Structure of apo-glycogenin truncated at residue 270==
<StructureSection load='3v8y' size='340' side='right' caption='[[3v8y]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3v8y' size='340' side='right'caption='[[3v8y]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v8y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V8Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V8Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ll0|1ll0]], [[1ll2|1ll2]], [[1ll3|1ll3]], [[1zct|1zct]], [[1zcu|1zcu]], [[1zcv|1zcv]], [[1zcy|1zcy]], [[3v8z|3v8z]], [[3v90|3v90]], [[3v91|3v91]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])</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=3v8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v8y OCA], [https://pdbe.org/3v8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v8y RCSB], [https://www.ebi.ac.uk/pdbsum/3v8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v8y 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/Glycogenin_glucosyltransferase Glycogenin glucosyltransferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v8y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v8y RCSB], [http://www.ebi.ac.uk/pdbsum/3v8y PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/GLYG_RABIT GLYG_RABIT] Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
The X-ray structure of rabbit glycogenin containing the T82M (T83M according to previous authors amino acid numbering [1]) mutation causing glycogenosis showed the loss of Thr82 hydrogen bond to Asp162, the residue involved in the activation step of the glucose transfer reaction mechanism. Autoglucosylation, maltoside transglucosylation and UDP-glucose hydrolyzing activities were abolished even though affinity and interactions with UDP-glucose and positioning of Tyr194 acceptor were conserved. Substitution of Thr82 for serine but not for valine restored the maximum extent of autoglucosylation as well as transglucosylation and UDP-glucose hydrolysis rate. Results provided evidence sustaining the essential role of the lost single hydrogen bond for UDP-glucose activation leading to glycogenin-bound glycogen primer synthesis.
 
Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.,Carrizo ME, Romero JM, Issoglio FM, Curtino JA FEBS Lett. 2012 Jan 3. PMID:22226635<ref>PMID:22226635</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Glycogenin|Glycogenin]]
*[[Glycogenin|Glycogenin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glycogenin glucosyltransferase]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Carrizo, M E]]
[[Category: Carrizo ME]]
[[Category: Curtino, J A]]
[[Category: Curtino JA]]
[[Category: Issoglio, F M]]
[[Category: Issoglio FM]]
[[Category: Romero, J M]]
[[Category: Romero JM]]
[[Category: Transferase]]

Latest revision as of 13:34, 1 March 2024

Structure of apo-glycogenin truncated at residue 270Structure of apo-glycogenin truncated at residue 270

Structural highlights

3v8y is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLYG_RABIT Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.

See Also

3v8y, resolution 2.15Å

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