2d5u: Difference between revisions

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OCA

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 ==Solution structure of the N-terminal portion of the PUB domain of mouse peptide:N-glycanase==
-<StructureSection load='2d5u' size='340' side='right'caption='[[2d5u]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2d5u' size='340' side='right'caption='[[2d5u]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d5u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D5U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D5U FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine_amidase Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.52 3.5.1.52] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5u OCA], [http://pdbe.org/2d5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d5u RCSB], [http://www.ebi.ac.uk/pdbsum/2d5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d5u 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=2d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5u OCA], [https://pdbe.org/2d5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d5u RCSB], [https://www.ebi.ac.uk/pdbsum/2d5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d5u ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/NGLY1_MOUSE NGLY1_MOUSE] Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.<ref>PMID:11562482</ref> <ref>PMID:12606569</ref> <ref>PMID:15358861</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 22: @@
 ==See Also==
 *[[Peptide N-glycanase|Peptide N-glycanase]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Hirao, T]]
+[[Category: Hirao T]]
-[[Category: Kato, K]]
+[[Category: Kato K]]
-[[Category: Sasakawa, H]]
+[[Category: Sasakawa H]]
-[[Category: Suzuki, T]]
+[[Category: Suzuki T]]
-[[Category: Yamaguchi, Y]]
+[[Category: Yamaguchi Y]]
-[[Category: Hydrolase]]
-[[Category: Pngase]]