Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE

• DOI: 10.1038/s41467-022-28722-w
• Publication Date: 2022-03-03T11:05:35Z
• Authors: Mikel García-Alija; Jonathan J. Du; Izaskun Ordóñez; Asier Diz-Vallenilla; Alicia Moraleda-M...; Nazneen Sultana; Chau G. Huynh; Chao Li; Thomas Connor Don...; Lai-Xi Wang; Beatriz Trastoy; Eric J. Sundberg; Marcelo E. Guerin
• Keywords: Endoglycosidase; Hydrolase

Abstract Bacteria produce a remarkably diverse range of glycoside hydrolases to metabolize glycans from the environment as primary source nutrients, and promote colonization infection host. Here we focus on EndoE, multi-modular hydrolase secreted by Enterococcus faecalis , one leading causes healthcare-associated infections. We provide X-ray crystal structures which show an architecture composed four domains, including GH18 GH20 connected two consecutive three α-helical bundles. determine that domain is exo-β-1,2- N -acetylglucosaminidase, whereas endo-β-1,4- -acetylglucosaminidase exclusively processes central core complex-type or high-mannose-type -glycans. Both domains act in concerted manner process -glycans glycoproteins, therapeutic IgG antibodies. EndoE combines enzyme with distinct functions glycan specificities play dual role metabolism immune evasion.