Backbone 1H, 13C, and 15N resonance assignments of BoMan26A, a β-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus
Autor: | Cecilia Persson, Santosh Kumar Upadhyay, Viktoria Bågenholm, Henrik Stålbrand, Sven Wernersson, Mikael Akke |
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Rok vydání: | 2019 |
Předmět: |
Polysaccharide utilization locus
Glycan 030303 biophysics Biochemistry Article Protein Structure Secondary 03 medical and health sciences Protein structure Structural Biology TIM barrel Bacteroides Humans Glycoside hydrolase Binding site Nuclear Magnetic Resonance Biomolecular 030304 developmental biology chemistry.chemical_classification Carbon Isotopes 0303 health sciences Nitrogen Isotopes biology beta-Mannosidase Substrate (chemistry) biology.organism_classification Gastrointestinal Microbiome Enzyme chemistry TIM-barrel biology.protein Protons β-Mannanase Bacteria |
Zdroj: | Biomolecular Nmr Assignments |
ISSN: | 1874-270X 1874-2718 |
Popis: | 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. |
Databáze: | OpenAIRE |
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