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6EUF

The GH43, Beta 1,3 Galactosidase, BT0265

Summary for 6EUF
Entry DOI10.2210/pdb6euf/pdb
DescriptorBeta-glucanase, alpha-L-arabinofuranose-(1-3)-[alpha-L-arabinofuranose-(1-4)][beta-D-glucopyranuronic acid-(1-6)]beta-D-galactopyranose-(1-6)-beta-D-galactopyranose, alpha-L-rhamnopyranose-(1-4)-beta-D-glucopyranuronic acid-(1-6)-[alpha-L-arabinofuranose-(1-3)][alpha-L-arabinofuranose-(1-4)]beta-D-galactopyranose-(1-6)-beta-D-galactopyranose, ... (4 entities in total)
Functional Keywordsarabiogalactan, gh43, beta 1, 3 galactosidase, hydrolase, hexasaccharide
Biological sourceBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Total number of polymer chains4
Total formula weight222108.41
Authors
Cartmell, A.,Gilbert, H.J. (deposition date: 2017-10-30, release date: 2018-10-17, Last modification date: 2024-05-08)
Primary citationCartmell, A.,Munoz-Munoz, J.,Briggs, J.A.,Ndeh, D.A.,Lowe, E.C.,Basle, A.,Terrapon, N.,Stott, K.,Heunis, T.,Gray, J.,Yu, L.,Dupree, P.,Fernandes, P.Z.,Shah, S.,Williams, S.J.,Labourel, A.,Trost, M.,Henrissat, B.,Gilbert, H.J.
A surface endogalactanase in Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation.
Nat Microbiol, 3:1314-1326, 2018
Cited by
PubMed Abstract: Glycans are major nutrients for the human gut microbiota (HGM). Arabinogalactan proteins (AGPs) comprise a heterogenous group of plant glycans in which a β1,3-galactan backbone and β1,6-galactan side chains are conserved. Diversity is provided by the variable nature of the sugars that decorate the galactans. The mechanisms by which nutritionally relevant AGPs are degraded in the HGM are poorly understood. Here we explore how the HGM organism Bacteroides thetaiotaomicron metabolizes AGPs. We propose a sequential degradative model in which exo-acting glycoside hydrolase (GH) family 43 β1,3-galactanases release the side chains. These oligosaccharide side chains are depolymerized by the synergistic action of exo-acting enzymes in which catalytic interactions are dependent on whether degradation is initiated by a lyase or GH. We identified two GHs that establish two previously undiscovered GH families. The crystal structures of the exo-β1,3-galactanases identified a key specificity determinant and departure from the canonical catalytic apparatus of GH43 enzymes. Growth studies of Bacteroidetes spp. on complex AGP revealed 3 keystone organisms that facilitated utilization of the glycan by 17 recipient bacteria, which included B. thetaiotaomicron. A surface endo-β1,3-galactanase, when engineered into B. thetaiotaomicron, enabled the bacterium to utilize complex AGPs and act as a keystone organism.
PubMed: 30349080
DOI: 10.1038/s41564-018-0258-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

237735

数据于2025-06-18公开中

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