Backbone 1H, 13C, and 15N resonance assignments of BoMan26A, a \u03b2-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus

Sven Wernersson,Henrik Stålbrand,Viktoria Bågenholm,Mikael Akke,Santosh Kumar Upadhyay,Cecilia Persson

doi:10.1007/s12104-019-09879-w

Sven Wernersson, Henrik Stålbrand + Show 4 more

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https://doi.org/10.1007/s12104-019-09879-w

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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 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.

Highlights

The β-mannanase BoMan26A is a glycoside hydrolase (GH) involved in dietary glycan hydrolysis by the common human gut bacterium Bacteroides ovatus (Bagenholm et al 2017)
It has been shown that the BoManPUL encodes GHs needed for the hydrolysis of galactomannan, i.e. two β-mannanases from family GH26 (BoMan26A, BoMan26B) and a family GH36 α-galactosidase (Reddy et al 2016; Bagenholm et al 2017)
The determination of the crystal structure of the periplasmic β-mannanase BoMan26A shed light on structural features that may be involved in the governance of mode of attack and product formation for this enzyme (Bagenholm et al 2017)

Summary

Introduction

The β-mannanase BoMan26A is a glycoside hydrolase (GH) involved in dietary glycan hydrolysis by the common human gut bacterium Bacteroides ovatus (Bagenholm et al 2017). 3 The Swedish NMR Center, University of Gothenburg, Gothenburg, Sweden attack and degradation of such glycans generally involves GHs. Members of Bacteroidetes often possess gene clusters known as polysaccharide utilization loci (PULs) which in concert encode the proteins needed for the utilization of a certain polymeric glycan (Martens et al 2009; Grondin et al 2017). Oligosaccharides are processed in the periplasm involving the β-mannanase BoMan26A (Bagenholm et al 2017).

Results

Conclusion