6DWO
Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583
Summary for 6DWO
| Entry DOI | 10.2210/pdb6dwo/pdb |
| Descriptor | Alpha-1,2-mannosidase, GLYCEROL, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | mannosidase, enterococcus faecalis, hydrolase |
| Biological source | Enterococcus faecalis (strain ATCC 700802 / V583) |
| Total number of polymer chains | 4 |
| Total formula weight | 333738.01 |
| Authors | Fisher, A.J.,Li, Y. (deposition date: 2018-06-26, release date: 2019-10-30, Last modification date: 2023-10-11) |
| Primary citation | Li, Y.,Li, R.,Yu, H.,Sheng, X.,Wang, J.,Fisher, A.J.,Chen, X. Enterococcus faecalis alpha 1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification. Febs Lett., 594:439-451, 2020 Cited by PubMed Abstract: While multiple α 1-2-mannosidases are necessary for glycoprotein N-glycan maturation in vertebrates, a single bacterial α1-2-mannosidase can be sufficient to cleave all α1-2-linked mannose residues in host glycoprotein N-glycans. We report here the characterization and crystal structure of a new α1-2-mannosidase (EfMan-I) from Enterococcus faecalis, a Gram-positive opportunistic human pathogen. EfMan-I catalyzes the cleavage of α1-2-mannose from not only oligomannoses but also high-mannose-type N-glycans on glycoproteins. Its 2.15 Å resolution crystal structure reveals a two-domain enzyme fold similar to other CAZy GH92 mannosidases. An unexpected potassium ion was observed bridging two domains near the active site. These findings support EfMan-I as an effective catalyst for in vitro N-glycan modification of glycoproteins with high-mannose-type N-glycans. PubMed: 31552675DOI: 10.1002/1873-3468.13618 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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