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.
Original language | English (US) |
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Journal | FEBS Letters |
DOIs | |
State | Accepted/In press - Jan 1 2019 |
Keywords
- alpha-mannosidase
- crystal structure
- glycoprotein modification
- mannosidase
- N-glycan enzymatic modification
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology