Dataset Information

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

ABSTRACT: 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 α-helical bundles. We determine that the GH20 domain is an exo-β-1,2-N-acetylglucosaminidase, whereas the GH18 domain is an endo-β-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.

SUBMITTER: Garcia-Alija M

PROVIDER: S-EPMC8894350 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature

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

García-Alija Mikel M Du Jonathan J JJ Ordóñez Izaskun I Diz-Vallenilla Asier A Moraleda-Montoya Alicia A Sultana Nazneen N Huynh Chau G CG Li Chao C Donahue Thomas Connor TC Wang Lai-Xi LX Trastoy Beatriz B Sundberg Eric J EJ Guerin Marcelo E ME

Nature communications 20220303 1

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 hydrola ...[more]

PMID: 35241669

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Dataset Information

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

Publications

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

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