7PUJ
Crystal structure of Endoglycosidase E GH18 domain from Enterococcus faecalis
Summary for 7PUJ
| Entry DOI | 10.2210/pdb7puj/pdb |
| Descriptor | Beta-N-acetylhexosaminidase, ZINC ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | glycoside hydrolase, gh18, glycan, antibody, enterococcus faecalis, endoe, hydrolase |
| Biological source | Enterococcus faecalis (Streptococcus faecalis) |
| Total number of polymer chains | 1 |
| Total formula weight | 49294.88 |
| Authors | Garcia-Alija, M.,Du, J.J.,Trastoy, B.,Sundberg, E.J.,Guerin, M.E. (deposition date: 2021-09-30, release date: 2022-03-16, Last modification date: 2024-01-31) |
| Primary citation | Garcia-Alija, M.,Du, J.J.,Ordonez, I.,Diz-Vallenilla, A.,Moraleda-Montoya, A.,Sultana, N.,Huynh, C.G.,Li, C.,Donahue, T.C.,Wang, L.X.,Trastoy, B.,Sundberg, E.J.,Guerin, M.E. Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE. Nat Commun, 13:1137-1137, 2022 Cited by PubMed 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. PubMed: 35241669DOI: 10.1038/s41467-022-28722-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.752 Å) |
Structure validation
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