5dl0
From Proteopedia
(Difference between revisions)
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==Crystal structure of glucosidase II alpha subunit (Glc1Man2-bound from)== | ==Crystal structure of glucosidase II alpha subunit (Glc1Man2-bound from)== | ||
<StructureSection load='5dl0' size='340' side='right' caption='[[5dl0]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5dl0' size='340' side='right' caption='[[5dl0]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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<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=5dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl0 OCA], [http://pdbe.org/5dl0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dl0 RCSB], [http://www.ebi.ac.uk/pdbsum/5dl0 PDBsum]</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=5dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl0 OCA], [http://pdbe.org/5dl0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dl0 RCSB], [http://www.ebi.ac.uk/pdbsum/5dl0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:26847925</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5dl0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:12, 20 February 2016
Crystal structure of glucosidase II alpha subunit (Glc1Man2-bound from)
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