6dwo

Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583

spinqualitylabelsall models 6dwo, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dwo is a 4 chain structure with sequence from Enterococcus faecalis V583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: ACT, CA, GOL, K, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q832K9_ENTFA Publication Abstract from PubMed While multiple alpha 1-2-mannosidases are necessary for glycoprotein N-glycan maturation in vertebrates, a single bacterial alpha1-2-mannosidase can be sufficient to cleave all alpha1-2-linked mannose residues in host glycoprotein N-glycans. We report here the characterization and crystal structure of a new alpha1-2-mannosidase (EfMan-I) from Enterococcus faecalis, a Gram-positive opportunistic human pathogen. EfMan-I catalyzes the cleavage of alpha1-2-mannose from not only oligomannoses but also high-mannose-type N-glycans on glycoproteins. Its 2.15 A 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. Enterococcus faecalis alpha1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification.,Li Y, Li R, Yu H, Sheng X, Wang J, Fisher AJ, Chen X FEBS Lett. 2019 Sep 25. doi: 10.1002/1873-3468.13618. PMID:31552675 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mannosidase 3D structures

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