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Backbone H-1, C-13, and N-15 resonance assignments of BoMan26A, a -mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus

Journal article
Authors S. Wernersson
V. Bagenholm
Cecilia Persson
S. K. Upadhyay
H. Stalbrand
M. Akke
Published in Biomolecular NMR Assignments
Volume 13
Issue 1
Pages 213-218
ISSN 1874-2718
Publication year 2019
Published at Swedish NMR Centre at Göteborg University
Pages 213-218
Language en
Links dx.doi.org/10.1007/s12104-019-09879...
Keywords Glycoside hydrolase, Polysaccharide utilization locus, -Mannanase, TIM-barrel, nmr-spectroscopy, microbiota
Subject categories Biochemistry and Molecular Biology, Physical Chemistry

Abstract

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 -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.

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