7LHA

Structure of the Exo-L-galactose-6-sulfatase BuS1_11 from Bacteroides uniformis

Summary for 7LHA

• Entry DOI: 10.2210/pdb7lha/pdb
• Descriptor: Exo-L-galactose-6-sulfatase, CALCIUM ION, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: sulfatase, porphyran, carbohydrate, hydrolase
• Biological source: Bacteroides uniformis
• Total number of polymer chains: 2
• Total formula weight: 124823.72

Authors

Robb, C.S.,Boraston, A.B. (deposition date: 2021-01-21, release date: 2022-02-09, Last modification date: 2023-10-18)

Primary citation

Robb, C.S.,Hobbs, J.K.,Pluvinage, B.,Reintjes, G.,Klassen, L.,Monteith, S.,Giljan, G.,Amundsen, C.,Vickers, C.,Hettle, A.G.,Hills, R.,Xing, X.,Montina, T.,Zandberg, W.F.,Abbott, D.W.,Boraston, A.B.
Metabolism of a hybrid algal galactan by members of the human gut microbiome.
Nat.Chem.Biol., 18:501-510, 2022

PubMed Abstract: Native 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.

PubMed: 35289327
DOI: 10.1038/s41589-022-00983-y

Experimental method

X-RAY DIFFRACTION (1.95 Å)