6M76

GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis

6M76 の概要

• エントリーDOI: 10.2210/pdb6m76/pdb
• 分子名称: LPXTG-motif cell wall anchor domain protein, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: glycoside hydrolase, mucin, (beta/alpha)8-barrel, fibronectin-like, hydrolase
• 由来する生物種: Enterococcus faecalis ATCC 10100
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 107187.25

構造登録者

Miyazaki, T. (登録日: 2020-03-17, 公開日: 2020-05-20, 最終更新日: 2024-03-27)

主引用文献

Miyazaki, T.,Park, E.Y.
Crystal structure of the Enterococcus faecalis alpha-N-acetylgalactosaminidase, a member of the glycoside hydrolase family 31.
Febs Lett., 594:2282-2293, 2020

PubMed Abstract: Glycoside hydrolases catalyze the hydrolysis of glycosidic linkages in carbohydrates. The glycoside hydrolase family 31 (GH31) contains α-glucosidase, α-xylosidase, α-galactosidase, and α-transglycosylase. Recent work has expanded the diversity of substrate specificity of GH31 enzymes, and α-N-acetylgalactosaminidases (αGalNAcases) belonging to GH31 have been identified in human gut bacteria. Here, we determined the first crystal structure of a truncated form of GH31 αGalNAcase from the human gut bacterium Enterococcus faecalis. The enzyme has a similar fold to other reported GH31 enzymes and an additional fibronectin type 3-like domain. Additionally, the structure in complex with N-acetylgalactosamine reveals that conformations of the active site residues, including its catalytic nucleophile, change to recognize the ligand. Our structural analysis provides insight into the substrate recognition and catalytic mechanism of GH31 αGalNAcases.

PubMed: 32367553
DOI: 10.1002/1873-3468.13804

実験手法

X-RAY DIFFRACTION (1.4 Å)