6dey: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6dey is ~~ON HOLD until Paper~~ Publication

==Aspartylglucosaminuria mutant structure and function==

== 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>

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Guo, H C]]

[[Category: Laksminarasimhan, D]]

[[Category: Pande, S]]

[[Category: Hydrolase]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6dey is ON HOLD  until Paper Publication
+==Aspartylglucosaminuria mutant structure and function==
+<StructureSection load='6dey' size='340' side='right' caption='[[6dey]], [[Resolution|resolution]] 1.63&Aring;' 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]