6dey
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Aspartylglucosaminuria mutant structure and function== | |
| + | <StructureSection load='6dey' size='340' side='right' caption='[[6dey]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6dey]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DEY FirstGlance]. <br> | ||
| + | </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=6dey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dey OCA], [http://pdbe.org/6dey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dey RCSB], [http://www.ebi.ac.uk/pdbsum/6dey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dey ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aspartylglucosaminuria (AGU) is a lysosomal storage disorder caused by defects of the hydrolase glycosylasparaginase (GA). Previously, we showed that a Canadian AGU mutation disrupts an obligatory intramolecular autoprocessing with the enzyme trapped as an inactive precursor. Here, we report biochemical and structural characterizations of a model enzyme corresponding to a Finnish AGU allele, the T234I variant. Unlike the Canadian counterpart, the Finnish variant is capable of a slow autoprocessing to generate detectible hydrolyzation activity of the natural substrate of GA. We have determined a 1.6 A-resolution structure of the Finnish AGU model and built an enzyme-substrate complex to provide a structural basis for analyzing the negative effects of the point mutation on KM and kcat of the mature enzyme. ENZYME: Glycosylasparaginase or aspartylglucosaminidase, EC3.5.1.26. | ||
| - | + | Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria.,Pande S, Bizilj W, Guo HC FEBS Lett. 2018 Jul 11. doi: 10.1002/1873-3468.13190. PMID:29993127<ref>PMID:29993127</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6dey" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Guo, H C]] | ||
| + | [[Category: Laksminarasimhan, D]] | ||
| + | [[Category: Pande, S]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 18:50, 1 August 2018
Aspartylglucosaminuria mutant structure and function
| |||||||||||
