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7EJT

Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (W470A) in complex with maltoheptaose

Summary for 7EJT
Entry DOI10.2210/pdb7ejt/pdb
Descriptor4-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 Keywordsglycogen debranching enzyme, sugar binding protein
Biological sourceCandida glabrata CBS 138 (Yeast, Torulopsis glabrata)
Total number of polymer chains2
Total formula weight354047.58
Authors
Shen, M.,Xiang, S. (deposition date: 2021-04-02, release date: 2021-11-10, Last modification date: 2023-11-29)
Primary citationShen, 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: 34726181
DOI: 10.1107/S2053230X21010918
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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