3v8y: Difference between revisions
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<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> | <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> | ||
== 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. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 07:43, 25 December 2014
Structure of apo-glycogenin truncated at residue 270Structure of apo-glycogenin 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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