7puj | pdb_00007puj

Crystal structure of Endoglycosidase E GH18 domain from Enterococcus faecalis

spinqualitylabelsall models 7puj, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7puj is a 1 chain structure with sequence from Enterococcus faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.752Å Ligands: CL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q839P8_ENTFA Publication Abstract from PubMed Bacteria produce a remarkably diverse range of glycoside hydrolases to metabolize glycans from the environment as a primary source of nutrients, and to promote the colonization and infection of a host. Here we focus on EndoE, a multi-modular glycoside hydrolase secreted by Enterococcus faecalis, one of the leading causes of healthcare-associated infections. We provide X-ray crystal structures of EndoE, which show an architecture composed of four domains, including GH18 and GH20 glycoside hydrolases connected by two consecutive three alpha-helical bundles. We determine that the GH20 domain is an exo-beta-1,2-N-acetylglucosaminidase, whereas the GH18 domain is an endo-beta-1,4-N-acetylglucosaminidase that exclusively processes the central core of complex-type or high-mannose-type N-glycans. Both glycoside hydrolase domains act in a concerted manner to process diverse N-glycans on glycoproteins, including therapeutic IgG antibodies. EndoE combines two enzyme domains with distinct functions and glycan specificities to play a dual role in glycan metabolism and immune evasion. Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE.,Garcia-Alija M, Du JJ, Ordonez I, Diz-Vallenilla A, Moraleda-Montoya A, Sultana N, Huynh CG, Li C, Donahue TC, Wang LX, Trastoy B, Sundberg EJ, Guerin ME Nat Commun. 2022 Mar 3;13(1):1137. doi: 10.1038/s41467-022-28722-w. PMID:35241669 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-N-acetylhexosaminidase 3D structures

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