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| | ==Crystal structure of Processing alpha-Glucosidase I== | | ==Crystal structure of Processing alpha-Glucosidase I== |
| - | <StructureSection load='4j5t' size='340' side='right' caption='[[4j5t]], [[Resolution|resolution]] 2.04Å' scene=''> | + | <StructureSection load='4j5t' size='340' side='right'caption='[[4j5t]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j5t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J5T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J5T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J5T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.04Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CWH41, GLS1, YGL027C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_glucosidase Mannosyl-oligosaccharide glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.106 3.2.1.106] </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=4j5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5t OCA], [https://pdbe.org/4j5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j5t RCSB], [https://www.ebi.ac.uk/pdbsum/4j5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5t 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=4j5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5t OCA], [http://pdbe.org/4j5t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j5t RCSB], [http://www.ebi.ac.uk/pdbsum/4j5t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CWH41_YEAST CWH41_YEAST]] Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically. Seems to play a role in beta-1,6-glucan synthesis. | + | [https://www.uniprot.org/uniprot/CWH41_YEAST CWH41_YEAST] Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically. Seems to play a role in beta-1,6-glucan synthesis. |
| | <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: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Mannosyl-oligosaccharide glucosidase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Barker, M K]] | + | [[Category: Barker MK]] |
| - | [[Category: Rose, D R]] | + | [[Category: Rose DR]] |
| - | [[Category: Er membrane]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: N-glycoprotein]]
| + | |
| Structural highlights
Function
CWH41_YEAST Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically. Seems to play a role in beta-1,6-glucan synthesis.
Publication Abstract from PubMed
Processing alpha-glucosidase I (GluI) is a key member of the eukaryotic N-glycosylation processing pathway, selectively catalyzing the first glycoprotein trimming step in the endoplasmic reticulum. Inhibition of GluI activity impacts the infectivity of enveloped viruses; however, despite interest in this protein from a structural, enzymatic, and therapeutic standpoint, little is known about its structure and enzymatic mechanism in catalysis of the unique glycan substrate Glc3Man9GlcNAc2. The first structural model of eukaryotic GluI is here presented at 2-A resolution. Two catalytic residues are proposed, mutations of which result in catalytically inactive, properly folded protein. Using Autodocking methods with the known substrate and inhibitors as ligands, including a novel inhibitor characterized in this work, the active site of GluI was mapped. From these results, a model of substrate binding has been formulated, which is most likely conserved in mammalian GluI.
Specificity of Processing alpha-Glucosidase I Is Guided by the Substrate Conformation: CRYSTALLOGRAPHIC AND IN SILICO STUDIES.,Barker MK, Rose DR J Biol Chem. 2013 May 10;288(19):13563-74. doi: 10.1074/jbc.M113.460436. Epub, 2013 Mar 27. PMID:23536181[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barker MK, Rose DR. Specificity of Processing alpha-Glucosidase I Is Guided by the Substrate Conformation: CRYSTALLOGRAPHIC AND IN SILICO STUDIES. J Biol Chem. 2013 May 10;288(19):13563-74. doi: 10.1074/jbc.M113.460436. Epub, 2013 Mar 27. PMID:23536181 doi:10.1074/jbc.M113.460436
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