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| | <StructureSection load='5d0f' size='340' side='right'caption='[[5d0f]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='5d0f' size='340' side='right'caption='[[5d0f]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canga Canga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D0F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D0F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CEX:ALPHA-D-GLUCOPYRANOSYL-(1- 4)-ALPHA-D-GLUCOPYRANOSYL-(1- 4)-ALPHA-D-GLUCOPYRANOSYL-(1- 4)-ALPHA-D-GLUCOPYRANOSYL-(1- 4)-ALPHA-D-GLUCOPYRANOSE'>CEX</scene>, <scene name='pdbligand=MLR:MALTOTRIOSE'>MLR</scene>, <scene name='pdbligand=MTT:MALTOTETRAOSE'>MTT</scene></td></tr> | + | </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_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=PRD_900030:alpha-maltopentaose'>PRD_900030</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d06|5d06]]</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=5d0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d0f OCA], [https://pdbe.org/5d0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d0f RCSB], [https://www.ebi.ac.uk/pdbsum/5d0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d0f ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAGL0G09977g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284593 CANGA])</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=5d0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d0f OCA], [http://pdbe.org/5d0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d0f RCSB], [http://www.ebi.ac.uk/pdbsum/5d0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d0f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6FSK0_CANGA Q6FSK0_CANGA] |
| | <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: Canga]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xiang, S]] | + | [[Category: Xiang S]] |
| - | [[Category: Zhai, L]] | + | [[Category: Zhai L]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
Q6FSK0_CANGA
Publication Abstract from PubMed
Glycogen is a branched glucose polymer and serves as an important energy store. Its debranching is a critical step in its mobilization. In animals and fungi, the 170 kDa glycogen debranching enzyme (GDE) catalyses this reaction. GDE deficiencies in humans are associated with severe diseases collectively termed glycogen storage disease type III (GSDIII). We report crystal structures of GDE and its complex with oligosaccharides, and structure-guided mutagenesis and biochemical studies to assess the structural observations. These studies reveal that distinct domains in GDE catalyse sequential reactions in glycogen debranching, the mechanism of their catalysis and highly specific substrate recognition. The unique tertiary structure of GDE provides additional contacts to glycogen besides its active sites, and our biochemical experiments indicate that they mediate its recruitment to glycogen and regulate its activity. Combining the understanding of the GDE catalysis and functional characterizations of its disease-causing mutations provides molecular insights into GSDIII.
Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations.,Zhai L, Feng L, Xia L, Yin H, Xiang S Nat Commun. 2016 Apr 18;7:11229. doi: 10.1038/ncomms11229. PMID:27088557[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhai L, Feng L, Xia L, Yin H, Xiang S. Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations. Nat Commun. 2016 Apr 18;7:11229. doi: 10.1038/ncomms11229. PMID:27088557 doi:http://dx.doi.org/10.1038/ncomms11229
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