5D06

Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme

5D06 の概要

• エントリーDOI: 10.2210/pdb5d06/pdb
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: tim barrel, (alpha/alpha)6 barrel, hydrolase, sugar binding protein
• 由来する生物種: Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 348946.84

構造登録者

Zhai, L.,Xiang, S. (登録日: 2015-08-02, 公開日: 2016-05-18, 最終更新日: 2024-11-13)

主引用文献

Zhai, L.,Feng, L.,Xia, L.,Yin, H.,Xiang, S.
Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations.
Nat Commun, 7:11229-11229, 2016

PubMed Abstract: Glycogen is a branched glucose polymer and serves as an important energy store. Its debranching is a critical step in its mobilization. In animals and fungi, the 170 kDa glycogen debranching enzyme (GDE) catalyses this reaction. GDE deficiencies in humans are associated with severe diseases collectively termed glycogen storage disease type III (GSDIII). We report crystal structures of GDE and its complex with oligosaccharides, and structure-guided mutagenesis and biochemical studies to assess the structural observations. These studies reveal that distinct domains in GDE catalyse sequential reactions in glycogen debranching, the mechanism of their catalysis and highly specific substrate recognition. The unique tertiary structure of GDE provides additional contacts to glycogen besides its active sites, and our biochemical experiments indicate that they mediate its recruitment to glycogen and regulate its activity. Combining the understanding of the GDE catalysis and functional characterizations of its disease-causing mutations provides molecular insights into GSDIII.

PubMed: 27088557
DOI: 10.1038/ncomms11229

実験手法

X-RAY DIFFRACTION (3.1 Å)