5MQR

Sialidase BT_1020

Summary for 5MQR

• Entry DOI: 10.2210/pdb5mqr/pdb
• Descriptor: Beta-L-arabinobiosidase, CALCIUM ION, TRIETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: sialidase, arabinofuranosidase, plant pectin, hydrolase
• Biological source: Bacteroides thetaiotaomicron
• Total number of polymer chains: 1
• Total formula weight: 130226.21

Authors

Basle, A.,Ndeh, D.,Rogowski, A.,Cartmell, A.,Luis, A.S.,Venditto, I.,Labourel, A.,Gilbert, H.J. (deposition date: 2016-12-20, release date: 2017-03-22, Last modification date: 2024-10-23)

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

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: 28329766
DOI: 10.1038/nature21725

Experimental method

X-RAY DIFFRACTION (2.2 Å)