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| | <StructureSection load='5dkz' size='340' side='right'caption='[[5dkz]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5dkz' size='340' side='right'caption='[[5dkz]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dkz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DKZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DKZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dkz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DKZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dkx|5dkx]], [[5dky|5dky]], [[5dl0|5dl0]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900052:alpha-nigerose'>PRD_900052</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0064960 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=5dkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dkz OCA], [https://pdbe.org/5dkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dkz RCSB], [https://www.ebi.ac.uk/pdbsum/5dkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dkz ProSAT]</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=5dkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dkz OCA], [http://pdbe.org/5dkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dkz RCSB], [http://www.ebi.ac.uk/pdbsum/5dkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dkz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0SG42_CHATD G0SG42_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kato, K]] | + | [[Category: Kato K]] |
| - | [[Category: Satoh, T]] | + | [[Category: Satoh T]] |
| - | [[Category: Toshimori, T]] | + | [[Category: Toshimori T]] |
| - | [[Category: Yamaguchi, T]] | + | [[Category: Yamaguchi T]] |
| - | [[Category: Yan, G]] | + | [[Category: Yan G]] |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
G0SG42_CHATD
Publication Abstract from PubMed
The endoplasmic reticulum (ER) has a sophisticated protein quality control system for the efficient folding of newly synthesized proteins. In this system, a variety of N-linked oligosaccharides displayed on proteins serve as signals recognized by series of intracellular lectins. Glucosidase II catalyzes two-step hydrolysis at alpha1,3-linked glucose-glucose and glucose-mannose residues of high-mannose-type glycans to generate a quality control protein tag that is transiently expressed on glycoproteins and recognized by ER chaperones. Here we determined the crystal structures of the catalytic alpha subunit of glucosidase II (GIIalpha) complexed with two different glucosyl ligands containing the scissile bonds of first- and second-step reactions. Our structural data revealed that the nonreducing terminal disaccharide moieties of the two kinds of substrates can be accommodated in a gourd-shaped bilocular pocket, thereby providing a structural basis for substrate-binding specificity in the two-step deglucosylation catalyzed by this enzyme.
Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.,Satoh T, Toshimori T, Yan G, Yamaguchi T, Kato K Sci Rep. 2016 Feb 5;6:20575. doi: 10.1038/srep20575. PMID:26847925[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Satoh T, Toshimori T, Yan G, Yamaguchi T, Kato K. Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control. Sci Rep. 2016 Feb 5;6:20575. doi: 10.1038/srep20575. PMID:26847925 doi:http://dx.doi.org/10.1038/srep20575
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