7EJT
Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (W470A) in complex with maltoheptaose
Summary for 7EJT
Entry DOI | 10.2210/pdb7ejt/pdb |
Descriptor | 4-alpha-glucanotransferase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | glycogen debranching enzyme, sugar binding protein |
Biological source | Candida glabrata CBS 138 (Yeast, Torulopsis glabrata) |
Total number of polymer chains | 2 |
Total formula weight | 354047.58 |
Authors | |
Primary citation | Shen, M.,Gong, X.,Xiang, S. Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides. Acta Crystallogr.,Sect.F, 77:420-426, 2021 Cited by PubMed Abstract: Debranching is a critical step in the mobilization of the important energy store glycogen. In eukaryotes, including fungi and animals, the highly conserved glycogen-debranching enzyme (GDE) debranches glycogen by a glucanotransferase (GT) reaction followed by a glucosidase (GC) reaction. Previous work indicated that these reactions are catalyzed by two active sites located more than 50 Å apart and provided insights into their catalytic mechanisms and substrate recognition. Here, five crystal structures of GDE in complex with oligosaccharides with 4-9 glucose residues are presented. The data suggest that the glycogen main chain plays a critical role in binding to the GT and GC active sites of GDE and that a minimum of five main-chain residues are required for optimal binding. PubMed: 34726181DOI: 10.1107/S2053230X21010918 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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