6GN6

Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus

6GN6 の概要

• エントリーDOI: 10.2210/pdb6gn6/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Alpha-L-fucosidase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: alpha-l-fucosidase, gh29, active site complementation, hexamer, hydrolase
• 由来する生物種: Paenibacillus thiaminolyticus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 314311.40

構造登録者

Kovalova, T.,Koval, T.,Lipovova, P.,Dohnalek, J. (登録日: 2018-05-30, 公開日: 2018-12-26, 最終更新日: 2024-01-17)

主引用文献

Kovalova, T.,Koval, T.,Benesova, E.,Vodickova, P.,Spiwok, V.,Lipovova, P.,Dohnalek, J.
Active site complementation and hexameric arrangement in the GH family 29; a structure-function study of alpha-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus.
Glycobiology, 29:59-73, 2019

PubMed Abstract: α-l-Fucosidase isoenzyme 1 from bacterium Paenibacillus thiaminolyticus is a member of the glycoside hydrolase family GH29 capable of cleaving l-fucose from nonreducing termini of oligosaccharides and glycoconjugates. Here we present the first crystal structure of this protein revealing a novel quaternary state within this family. The protein is in a unique hexameric assembly revealing the first observed case of active site complementation by a residue from an adjacent monomer in this family. Mutation of the complementing tryptophan residue caused changes in the catalytic properties including a shift of the pH optimum, a change of affinity to an artificial chromogenic substrate and a decreased reaction rate for a natural substrate. The wild-type enzyme was active on most of the tested naturally occurring oligosaccharides and capable of transglycosylation on a variety of acceptor molecules, including saccharides, alcohols or chromogenic substrates. Mutation of the complementing residue changed neither substrate specificity nor the preference for the type of transglycosylation acceptor molecule; however, the yields of the reactions were lower in both cases. Maltose molecules bound to the enzyme in the crystal structure identified surface carbohydrate-binding sites, possibly participating in binding of larger oligosaccharides.

PubMed: 30544181
DOI: 10.1093/glycob/cwy078

実験手法

X-RAY DIFFRACTION (2.2 Å)