1apz
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1apz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1apz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APZ FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1apz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apz OCA], [https://pdbe.org/1apz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apz RCSB], [https://www.ebi.ac.uk/pdbsum/1apz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apz 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=1apz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apz OCA], [https://pdbe.org/1apz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apz RCSB], [https://www.ebi.ac.uk/pdbsum/1apz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | + | [https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[https://omim.org/entry/208400 208400]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref> | |
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1apz ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1apz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits. Two alpha- and beta-chains are found to pack together forming the final heterotetrameric structure. The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site. On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum. The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease. | ||
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| - | Three-dimensional structure of human lysosomal aspartylglucosaminidase.,Oinonen C, Tikkanen R, Rouvinen J, Peltonen L Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222<ref>PMID:8846222</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1apz" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Oinonen | + | [[Category: Oinonen C]] |
| - | [[Category: Rouvinen | + | [[Category: Rouvinen J]] |
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Revision as of 15:27, 13 March 2024
HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT
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