5MQO

Glycoside hydrolase BT_1003

5MQO の概要

• エントリーDOI: 10.2210/pdb5mqo/pdb
• 分子名称: Non-reducing end beta-L-arabinofuranosidase (1 entity in total)
• 機能のキーワード: glycoside hydrolase, aceric acidase, plant pectin, cazy family gh127, hydrolase
• 由来する生物種: Bacteroides thetaiotaomicron
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 78164.73

構造登録者

Basle, A.,Ndeh, D.,Rogowski, A.,Cartmell, A.,Luis, A.S.,Venditto, I.,Labourel, A.,Gilbert, H.J. (登録日: 2016-12-20, 公開日: 2017-03-22, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)