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    Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides

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    Author
    Du, J.J.
    Klontz, E.H.
    Sundberg, E.J.
    Date
    2020
    Journal
    Nature communications
    Publisher
    Springer Nature
    Type
    Article
    
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    See at
    https://doi.org/10.1038/s41467-020-14754-7
    Abstract
    The human gut microbiota plays a central role not only in regulating the metabolism of nutrients but also promoting immune homeostasis, immune responses and protection against pathogen colonization. The genome of the Gram-negative symbiont Bacteroides thetaiotaomicron, a dominant member of the human intestinal microbiota, encodes polysaccharide utilization loci PULs, the apparatus required to orchestrate the degradation of a specific glycan. EndoBT-3987 is a key endo-β-N-acetylglucosaminidase (ENGase) that initiates the degradation/processing of mammalian high-mannose-type (HM-type) N-glycans in the intestine. Here, we provide structural snapshots of EndoBT-3987, including the unliganded form, the EndoBT-3987-Man9GlcNAc2Asn substrate complex, and two EndoBT-3987-Man9GlcNAc and EndoBT-3987-Man5GlcNAc product complexes. In combination with alanine scanning mutagenesis and activity measurements we unveil the molecular mechanism of HM-type recognition and specificity for EndoBT-3987 and an important group of the GH18 ENGases, including EndoH, an enzyme extensively used in biotechnology, and for which the mechanism of substrate recognition was largely unknown.
    Keyword
    glycans
    Glycomics
    Crystallography, X-Ray
    Polysaccharides
    Gastrointestinal Microbiome
    Bacteroides thetaiotaomicron
    Identifier to cite or link to this item
    https://www.scopus.com/inward/record.uri?eid=2-s2.0-85079361800&doi=10.1038%2fs41467-020-14754-7&partnerID=40&md5=1281952b8bd63f553e65eb0ca2a86f7d; http://hdl.handle.net/10713/12127
    ae974a485f413a2113503eed53cd6c53
    10.1038/s41467-020-14754-7
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