5MSX
Glycoside hydrolase BT_3662
Summary for 5MSX
| Entry DOI | 10.2210/pdb5msx/pdb |
| Descriptor | Putative endo-1,4-beta-xylanase, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | glycoside hydrolase, gh43, arabinofuranosidase, plant pectin, rgii, hydrolase |
| Biological source | Bacteroides thetaiotaomicron VPI-5482 |
| Total number of polymer chains | 3 |
| Total formula weight | 158668.41 |
| Authors | Basle, A.,Ndeh, D.,Rogowski, A.,Cartmell, A.,Luis, A.S.,Venditto, I.,Labourel, A.,Gilbert, H.J. (deposition date: 2017-01-06, release date: 2017-03-22, Last modification date: 2024-01-17) |
| Primary citation | Ndeh, D.,Rogowski, A.,Cartmell, A.,Luis, A.S.,Basle, A.,Gray, J.,Venditto, I.,Briggs, J.,Zhang, X.,Labourel, A.,Terrapon, N.,Buffetto, F.,Nepogodiev, S.,Xiao, Y.,Field, R.A.,Zhu, Y.,O'Neill, M.A.,Urbanowicz, B.R.,York, W.S.,Davies, G.J.,Abbott, D.W.,Ralet, M.C.,Martens, E.C.,Henrissat, B.,Gilbert, H.J. Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature, 544:65-70, 2017 Cited by PubMed Abstract: The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron uses the most structurally complex glycan known: the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but 1 of its 21 distinct glycosidic linkages. The deconstruction of rhamnogalacturonan-II side chains and backbone are coordinated to overcome steric constraints, and the degradation involves previously undiscovered enzyme families and catalytic activities. The degradation system informs revision of the current structural model of rhamnogalacturonan-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycan in the human diet. PubMed: 28329766DOI: 10.1038/nature21725 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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