4r4y: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4r4y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_miricola Elizabethkingia miricola]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4R4Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[4r4y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_miricola Elizabethkingia miricola]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4R4Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SD4:N-HYDROXY-L-ASPARAGINE'>SD4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SD4:N-HYDROXY-L-ASPARAGINE'>SD4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r4y OCA], [https://pdbe.org/4r4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r4y RCSB], [https://www.ebi.ac.uk/pdbsum/4r4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r4y ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r4y OCA], [https://pdbe.org/4r4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r4y RCSB], [https://www.ebi.ac.uk/pdbsum/4r4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r4y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/ASPG_ELIMR ASPG_ELIMR] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.
[https://www.uniprot.org/uniprot/ASPG_ELIMR ASPG_ELIMR] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4r4y" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
*[[Glycosylasparaginase|Glycosylasparaginase]]
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 15:50, 1 March 2024

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

4r4y is a 2 chain structure with sequence from Elizabethkingia miricola. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASPG_ELIMR Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.

See Also

4r4y, resolution 2.10Å

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OCA
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