7EIM

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

7EIM の概要

• エントリーDOI: 10.2210/pdb7eim/pdb
• 分子名称: 4-alpha-glucanotransferase, alpha-D-glucopyranose-(1-4)-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 (3 entities in total)
• 機能のキーワード: glycogen debranching enzyme, sugar binding protein
• 由来する生物種: Candida glabrata CBS 138 (Yeast, Torulopsis glabrata)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 353885.44

構造登録者

Shen, M.,Xiang, S. (登録日: 2021-03-31, 公開日: 2021-11-10, 最終更新日: 2023-11-29)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (3.1 Å)