4r4y: Difference between revisions
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''' | ==Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria== | ||
<StructureSection load='4r4y' size='340' side='right' caption='[[4r4y]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r4y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R4Y FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SD4:N-HYDROXY-L-ASPARAGINE'>SD4</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </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=4r4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r4y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r4y RCSB], [http://www.ebi.ac.uk/pdbsum/4r4y PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aspartylglucosaminuria (AGU) is a lysosomal storage disease caused by a metabolic disorder of lysosomes to digest Asn-linked glycoproteins. The specific enzyme linked to AGU is a lysosomal hydrolase called glycosylasparaginase. Crystallographic studies revealed that a surface loop blocks the catalytic center of the mature hydrolase. Autoproteolysis is therefore required to remove this P loop and open up the hydrolase center. Nonetheless, AGU mutations result in misprocessing of their precursors and are deficient in hydrolyzing glycoasparagines. To understand the catalytic and structural consequences of AGU mutations, we have characterized two AGU models, one corresponding to a Finnish allele and the other found in a Canadian family. We also report a 2.1 A resolution structure of the latter AGU model. The current crystallographic study provides a high-resolution structure of an AGU mutant. It reveals substantial conformation changes at the defective autocleavage site of the AGU mutant, which is trapped as an inactive precursor. | |||
Structural Basis of a Point Mutation that Causes the Genetic Disease Aspartylglucosaminuria.,Sui L, Lakshminarasimhan D, Pande S, Guo HC Structure. 2014 Dec 2;22(12):1855-61. doi: 10.1016/j.str.2014.09.014. Epub 2014, Nov 13. PMID:25456816<ref>PMID:25456816</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Damodharan, L]] | |||
[[Category: Guo, H C]] | |||
[[Category: Pande, S]] | |||
[[Category: Sui, L]] | |||
[[Category: Agu structure]] | |||
[[Category: Autoprocessing]] | |||
[[Category: Glycosylasparaginase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Lysosomal storage disease]] | |||
[[Category: Pre-autoproteolysis trap]] | |||
Revision as of 15:47, 17 December 2014
Structural basis of a point mutation that causes the genetic disease AspartylglucosaminuriaStructural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria
Structural highlights
Publication Abstract from PubMedAspartylglucosaminuria (AGU) is a lysosomal storage disease caused by a metabolic disorder of lysosomes to digest Asn-linked glycoproteins. The specific enzyme linked to AGU is a lysosomal hydrolase called glycosylasparaginase. Crystallographic studies revealed that a surface loop blocks the catalytic center of the mature hydrolase. Autoproteolysis is therefore required to remove this P loop and open up the hydrolase center. Nonetheless, AGU mutations result in misprocessing of their precursors and are deficient in hydrolyzing glycoasparagines. To understand the catalytic and structural consequences of AGU mutations, we have characterized two AGU models, one corresponding to a Finnish allele and the other found in a Canadian family. We also report a 2.1 A resolution structure of the latter AGU model. The current crystallographic study provides a high-resolution structure of an AGU mutant. It reveals substantial conformation changes at the defective autocleavage site of the AGU mutant, which is trapped as an inactive precursor. Structural Basis of a Point Mutation that Causes the Genetic Disease Aspartylglucosaminuria.,Sui L, Lakshminarasimhan D, Pande S, Guo HC Structure. 2014 Dec 2;22(12):1855-61. doi: 10.1016/j.str.2014.09.014. Epub 2014, Nov 13. PMID:25456816[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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