5ta7 | pdb_00005ta7

Crystal structure of BuGH117Bwt

spinqualitylabelsall models 5ta7, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ta7 is a 2 chain structure with sequence from Atcc 8492. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, MG, TRS Related: 5ta0, 5ta1, 5ta5, 5ta9, 5t9x, 5t9g, 5t9a, 5t99, 5t98 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In red algae, the most abundant principal cell wall polysaccharides are mixed galactan agars, of which agarose is a common component. While bioconversion of agarose is predominantly catalyzed by bacteria that live in the oceans, agarases have been discovered in microorganisms that inhabit diverse terrestrial ecosystems, including human intestines. Here we comprehensively define the structure-function relationship of the agarolytic pathway from the human intestinal bacterium Bacteroides uniformis (Bu) NP1. Using recombinant agarases from Bu NP1 to completely depolymerize agarose, we demonstrate that a non-agarolytic Bu strain can grow on GAL released from agarose. This relationship underscores that rare nutrient utilization by intestinal bacteria is facilitated by the acquisition of highly specific enzymes that unlock inaccessible carbohydrate resources contained within unusual polysaccharides. Intriguingly, the agarolytic pathway is differentially distributed throughout geographically distinct human microbiomes, reflecting a complex historical context for agarose consumption by human beings. Molecular basis of an agarose metabolic pathway acquired by a human intestinal symbiont.,Pluvinage B, Grondin JM, Amundsen C, Klassen L, Moote PE, Xiao Y, Thomas D, Pudlo NA, Anele A, Martens EC, Inglis GD, Uwiera RER, Boraston AB, Abbott DW Nat Commun. 2018 Mar 13;9(1):1043. doi: 10.1038/s41467-018-03366-x. PMID:29535379 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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