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