5D0F
Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose
Summary for 5D0F
| Entry DOI | 10.2210/pdb5d0f/pdb |
| Related | 5D06 |
| Related PRD ID | PRD_900009 PRD_900010 PRD_900030 |
| Descriptor | Uncharacterized protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | tim barrel, (alpha/alpha)6 barrel, hydrolase, sugar binding protein |
| Biological source | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 356601.49 |
| Authors | |
| Primary citation | 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, 7:11229-11229, 2016 Cited by PubMed Abstract: 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. PubMed: 27088557DOI: 10.1038/ncomms11229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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