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Structure of the Exo-alpha-L-galactosidase BpGH29 from Bacteroides plebeius
Structural highlights
FunctionB5CYA5_PHOPM Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.[ARBA:ARBA00004071] Publication Abstract from PubMedNative porphyran is a hybrid of porphryan and agarose. As a common element of edible seaweed, this algal galactan is a frequent component of the human diet. Bacterial members of the human gut microbiota have acquired polysaccharide utilization loci (PULs) that enable the metabolism of porphyran or agarose. However, the molecular mechanisms that underlie the deconstruction and use of native porphyran remains incompletely defined. Here, we have studied two human gut bacteria, porphyranolytic Bacteroides plebeius and agarolytic Bacteroides uniformis, that target native porphyran. This reveals an exo-based cycle of porphyran depolymerization that incorporates a keystone sulfatase. In both PULs this cycle also works together with a PUL-encoded agarose depolymerizing machinery to synergistically reduce native porphyran to monosaccharides. This provides a framework for understanding the deconstruction of a hybrid algal galactan, and insight into the competitive and/or syntrophic relationship of gut microbiota members that target rare nutrients. Metabolism of a hybrid algal galactan by members of the human gut microbiome.,Robb CS, Hobbs JK, Pluvinage B, Reintjes G, Klassen L, Monteith S, Giljan G, Amundsen C, Vickers C, Hettle AG, Hills R, Nitin, Xing X, Montina T, Zandberg WF, Abbott DW, Boraston AB Nat Chem Biol. 2022 Mar 14. pii: 10.1038/s41589-022-00983-y. doi:, 10.1038/s41589-022-00983-y. PMID:35289327[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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