3v90: Difference between revisions
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==Structure of T82M glycogenin mutant truncated at residue 270== | ==Structure of T82M glycogenin mutant truncated at residue 270== | ||
<StructureSection load='3v90' size='340' side='right' caption='[[3v90]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3v90' size='340' side='right'caption='[[3v90]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v90]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3v90]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. 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='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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ll0|1ll0]], [[1ll2|1ll2]], [[1ll3|1ll3]], [[1zct|1zct]], [[1zcu|1zcu]], [[1zcv|1zcv]], [[1zcy|1zcy]], [[3v8y|3v8y]], [[3v8z|3v8z]], [[3v91|3v91]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([ | <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=9986 European rabbit])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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'>[ | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: European rabbit]] | [[Category: European rabbit]] | ||
[[Category: Glycogenin glucosyltransferase]] | [[Category: Glycogenin glucosyltransferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Carrizo, M E]] | [[Category: Carrizo, M E]] | ||
[[Category: Curtino, J A]] | [[Category: Curtino, J A]] | ||
Revision as of 11:41, 20 July 2022
Structure of T82M glycogenin mutant truncated at residue 270Structure of T82M glycogenin mutant truncated at residue 270
Structural highlights
Function[GLYG_RABIT] Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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