3v90

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Structure of T82M glycogenin mutant truncated at residue 270

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 ==Structure of T82M glycogenin mutant truncated at residue 270==
-<StructureSection load='3v90' size='340' side='right' caption='[[3v90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3v90' size='340' side='right'caption='[[3v90]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3v90]] 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=3V90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V90 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3v90]] 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=3V90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V90 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&#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]], [[3v8y|3v8y]], [[3v8z|3v8z]], [[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=3v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v90 OCA], [https://pdbe.org/3v90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v90 RCSB], [https://www.ebi.ac.uk/pdbsum/3v90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v90 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=3v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v90 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v90 RCSB], [http://www.ebi.ac.uk/pdbsum/3v90 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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==
 *[[Glycogenin|Glycogenin]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Glycogenin glucosyltransferase]]
+[[Category: Large Structures]]
 [[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]]

3v90

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Structure of T82M glycogenin mutant truncated at residue 270

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