6M77
GH31 alpha-N-acetylgalactosaminidase from Enterococcus faecalis in complex with N-acetylgalactosamine
Summary for 6M77
| Entry DOI | 10.2210/pdb6m77/pdb |
| Descriptor | LPXTG-motif cell wall anchor domain protein, 2-acetamido-2-deoxy-beta-D-galactopyranose, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | glycoside hydrolase, mucin, (beta/alpha)8-barrel, fibronectin-like, hydrolase |
| Biological source | Enterococcus faecalis ATCC 10100 |
| Total number of polymer chains | 1 |
| Total formula weight | 107200.27 |
| Authors | Miyazaki, T. (deposition date: 2020-03-17, release date: 2020-05-20, Last modification date: 2023-11-29) |
| Primary citation | 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 Cited by 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: 32367553DOI: 10.1002/1873-3468.13804 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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