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1apz

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[[Image:1apz.gif|left|200px]]<br />
 
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<applet load="1apz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1apz, resolution 2.3&Aring;" />
 
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'''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT'''<br />
 
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==Overview==
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==HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT==
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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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<StructureSection load='1apz' size='340' side='right'caption='[[1apz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Disease ==
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[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>
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== Function ==
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[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Aspartylglucosaminuria OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=208400 208400]]
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*[[Glycosylasparaginase|Glycosylasparaginase]]
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== References ==
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==About this Structure==
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<references/>
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1APZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and ASP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Sites: B and D. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846222 8846222]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Oinonen C]]
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[[Category: Oinonen, C.]]
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[[Category: Rouvinen J]]
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[[Category: Rouvinen, J.]]
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[[Category: ASP]]
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[[Category: NAG]]
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[[Category: aspartylglucosaminidase]]
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[[Category: complex (hydrolase/peptide)]]
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[[Category: glycosylasparaginase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:01:04 2007''
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Current revision

HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT

PDB ID 1apz

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