7D9C

Alpha-glucosidase from Weissella cibaria BBK-1 bound with maltose

7D9C の概要

• エントリーDOI: 10.2210/pdb7d9c/pdb
• 関連するPDBエントリー: 7D9B
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Alpha-glycosidase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (8 entities in total)
• 機能のキーワード: glycoside hydrolase, maltooligosaccharides, carbohydrate metabolism, hydrolase
• 由来する生物種: Weissella confusa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 70108.16

構造登録者

Krusong, K.,Wangpaiboon, K.,Kim, S.,Mori, T.,Hakoshima, T. (登録日: 2020-10-13, 公開日: 2021-08-11, 最終更新日: 2023-11-29)

主引用文献

Wangpaiboon, K.,Laohawuttichai, P.,Kim, S.Y.,Mori, T.,Nakapong, S.,Pichyangkura, R.,Pongsawasdi, P.,Hakoshima, T.,Krusong, K.
A GH13 alpha-glucosidase from Weissella cibaria uncommonly acts on short-chain maltooligosaccharides.
Acta Crystallogr D Struct Biol, 77:1064-1076, 2021

PubMed Abstract: α-Glucosidase (EC 3.2.1.20) is a carbohydrate-hydrolyzing enzyme which generally cleaves α-1,4-glycosidic bonds of oligosaccharides and starch from the nonreducing ends. In this study, the novel α-glucosidase from Weissella cibaria BBK-1 (WcAG) was biochemically and structurally characterized. WcAG belongs to glycoside hydrolase family 13 (GH13) and to the neopullanase subfamily. It exhibits distinct hydrolytic activity towards the α-1,4 linkages of short-chain oligosaccharides from the reducing end. The enzyme prefers to hydrolyse maltotriose and acarbose, while it cannot hydrolyse cyclic oligosaccharides and polysaccharides. In addition, WcAG can cleave pullulan hydrolysates and strongly exhibits transglycosylation activity in the presence of maltose. Size-exclusion chromatography and X-ray crystal structures revealed that WcAG forms a homodimer in which the N-terminal domain of one monomer is orientated in proximity to the catalytic domain of another, creating the substrate-binding groove. Crystal structures of WcAG in complexes with maltose, maltotriose and acarbose revealed a remarkable enzyme active site with accessible +2, +1 and -1 subsites, along with an Arg-Glu gate (Arg176-Glu296) in front of the active site. The -2 and -3 subsites were blocked by Met119 and Asn120 from the N-terminal domain of a different subunit, resulting in an extremely restricted substrate preference.

PubMed: 34342279
DOI: 10.1107/S205979832100677X

実験手法

X-RAY DIFFRACTION (1.36 Å)