Bacteroides ovatus is a member of the human gut microbiota. The importance of this microbial consortium involves the degradation of complex dietary glycans mainly conferred by glycoside hydrolases. In this study we focus on one such catabolic glycoside hydrolase from B. ovatus. The enzyme, termed BoMan26A, is a β-mannanase that takes part in the hydrolytic degradation of galactomannans. The crystal structure of BoMan26A has previously been determined to reveal a TIM-barrel like fold, but the relation between the protein structure and the mode of substrate processing has not yet been studied. Here we report residue-specific assignments for 95% of the 344 backbone amides of BoMan26A. The assignments form the basis for future studies of the relationship between substrate interactions and protein dynamics. In particular, the potential role of loops adjacent to glycan binding sites is of interest for such studies.

中文翻译：

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BoMan26A 的骨架 1H、13C 和 15N 共振分配，BoMan26A 是来自人肠道细菌卵形拟杆菌的糖苷水解酶家族 26 的 β-甘露聚糖酶。

卵形拟杆菌是人类肠道微生物群的成员。这种微生物聚生体的重要性涉及主要由糖苷水解酶赋予的复杂膳食聚糖的降解。在这项研究中，我们专注于一种来自B. ovatus 的分解代谢糖苷水解酶. 该酶称为 BoMan26A，是一种 β-甘露聚糖酶，参与半乳甘露聚糖的水解降解。BoMan26A 的晶体结构先前已被确定为揭示 TIM 桶状折叠，但尚未研究蛋白质结构与底物加工模式之间的关系。在这里，我们报告了 BoMan26A 的 344 个主链酰胺中 95% 的残基特异性分配。这些分配构成了未来研究底物相互作用和蛋白质动力学之间关系的基础。特别是，与聚糖结合位点相邻的环的潜在作用是此类研究的兴趣所在。