{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shen M"],"funding":["Natural Science Foundation of China","National Natural Science Foundation of China"],"pagination":["420-426"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8561817"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["77(Pt 11)"],"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."],"journal":["Acta crystallographica. Section F, Structural biology communications"],"pubmed_title":["Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides."],"pmcid":["PMC8561817"],"funding_grant_id":["32071205","31870769"],"pubmed_authors":["Shen M","Xiang S","Gong X"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides.","description":"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.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2025-04-04T22:32:13.71Z","creation":"2025-02-19T03:24:06.174Z"},"accession":"S-EPMC8561817","cross_references":{"pubmed":["34726181"],"doi":["10.1107/s2053230x21010918","10.1107/S2053230X21010918"]}}