4AIO

Crystal structure of the starch debranching enzyme barley limit dextrinase

4AIO の概要

• エントリーDOI: 10.2210/pdb4aio/pdb
• 分子名称: LIMIT DEXTRINASE, GLYCEROL, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, pullulanase, glycoside hydrolase family 13
• 由来する生物種: HORDEUM VULGARE (BARLEY)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 98400.30

構造登録者

Moeller, M.S.,Abou Hachem, M.,Svensson, B.,Henriksen, A. (登録日: 2012-02-11, 公開日: 2012-08-15, 最終更新日: 2023-12-20)

主引用文献

Moeller, M.S.,Abou Hachem, M.,Svensson, B.,Henriksen, A.
Structure of the Starch-Debranching Enzyme Barley Limit Dextrinase Reveals Homology of the N-Terminal Domain to Cbm21.
Acta Crystallogr.,Sect.F, 68:1008-, 2012

PubMed Abstract: Barley limit dextrinase (HvLD) is a debranching enzyme from glycoside hydrolase family 13 subfamily 13 (GH13_13) that hydrolyses α-1,6-glucosidic linkages in limit dextrins derived from amylopectin. The structure of HvLD was solved and refined to 1.9 Å resolution. The structure has a glycerol molecule in the active site and is virtually identical to the structures of HvLD in complex with the competitive inhibitors α-cyclodextrin and β-cyclodextrin solved to 2.5 and 2.1 Å resolution, respectively. However, three loops in the N-terminal domain that are shown here to resemble carbohydrate-binding module family 21 were traceable and were included in the present HvLD structure but were too flexible to be traced and included in the structures of the two HvLD-inhibitor complexes.

PubMed: 22949184
DOI: 10.1107/S1744309112031004

実験手法

X-RAY DIFFRACTION (1.9 Å)