Structural highlights
Publication Abstract from PubMed
Glycoside hydrolases catalyze the hydrolysis of glycosidic linkages in carbohydrates. The glycoside hydrolase family 31 (GH31) contains alpha-glucosidase, alpha-xylosidase, alpha-galactosidase, and alpha-transglycosylase. Recent work has expanded the diversity of substrate specificity of GH31 enzymes, and alpha-N-acetylgalactosaminidases (alphaGalNAcases) belonging to GH31 have been identified in human gut bacteria. Here, we determined the first crystal structure of a truncated form of GH31 alphaGalNAcase 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 alphaGalNAcases.
Crystal structure of the Enterococcus faecalis alpha-N-acetylgalactosaminidase, a member of the glycoside hydrolase family 31.,Miyazaki T, Park EY FEBS Lett. 2020 May 4. doi: 10.1002/1873-3468.13804. PMID:32367553[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyazaki T, Park EY. Crystal structure of the Enterococcus faecalis alpha-N-acetylgalactosaminidase, a member of the glycoside hydrolase family 31. FEBS Lett. 2020 May 4. doi: 10.1002/1873-3468.13804. PMID:32367553 doi:http://dx.doi.org/10.1002/1873-3468.13804
