8va3
Crystal structure of CapGH3b enzyme retrieved from capybara gut metagenomeCrystal structure of CapGH3b enzyme retrieved from capybara gut metagenome
Structural highlights
Publication Abstract from PubMedGut microbiota members from the Bacteroidota phylum play a pivotal role in mammalian health and metabolism. They thrive in this diverse ecosystem due to their notable ability to cope with distinct recalcitrant dietary glycans via polysaccharide utilization loci (PULs). Our study reveals that a PUL from an herbivore gut bacterium belonging to the Bacteroidota phylum, with a gene composition similar to that in the human gut, exhibits extended functionality. While the human gut PUL targets mixed-linkage beta-glucans specifically, the herbivore gut PUL also efficiently processes linear and substituted beta-1,3-glucans. This gain of function emerges from molecular adaptations in recognition proteins and carbohydrate-active enzymes, including a beta-glucosidase specialized for beta(1,6)-glucosyl linkages, a typical substitution in beta(1,3)-glucans. These findings broaden the existing model for non-cellulosic beta-glucans utilization by gut bacteria, revealing an additional layer of functional and evolutionary complexity within the gut microbiota, beyond conventional gene insertions/deletions to intricate biochemical interactions. A functionally augmented carbohydrate utilization locus from herbivore gut microbiota fueled by dietary beta-glucans.,Mandelli F, Martins MP, Chinaglia M, Lima EA, Morais MAB, Lima TB, Cabral L, Pirolla RAS, Fuzita FJ, Paixao DAA, Andrade MO, Wolf LD, Vieira PS, Persinoti GF, Murakami MT NPJ Biofilms Microbiomes. 2024 Oct 14;10(1):105. doi: 10.1038/s41522-024-00578-6. PMID:39397008[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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