Advanced

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

Wernersson, Sven LU ; Bågenholm, Viktoria LU ; Persson, Cecilia; Upadhyay, Santosh Kumar; Stålbrand, Henrik LU and Akke, Mikael LU (2019) In Biomolecular NMR Assignments
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... (More)

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.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
epub
subject
keywords
Glycoside hydrolase, Polysaccharide utilization locus, TIM-barrel, β-Mannanase
in
Biomolecular NMR Assignments
publisher
Springer
external identifiers
  • scopus:85061254285
ISSN
1874-2718
DOI
10.1007/s12104-019-09879-w
language
English
LU publication?
yes
id
054fd628-a967-4948-8762-e6d296908c65
date added to LUP
2019-02-20 09:51:20
date last changed
2019-03-19 04:05:43
@article{054fd628-a967-4948-8762-e6d296908c65,
  abstract     = {<p>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.</p>},
  author       = {Wernersson, Sven and Bågenholm, Viktoria and Persson, Cecilia and Upadhyay, Santosh Kumar and Stålbrand, Henrik and Akke, Mikael},
  issn         = {1874-2718},
  keyword      = {Glycoside hydrolase,Polysaccharide utilization locus,TIM-barrel,β-Mannanase},
  language     = {eng},
  month        = {02},
  publisher    = {Springer},
  series       = {Biomolecular NMR Assignments},
  title        = {Backbone                          
                        <sup>1</sup>
                                                 H,                          
                        <sup>13</sup>
                                                 C, and                          
                        <sup>15</sup>
                                                 N resonance assignments of BoMan26A, a β-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus},
  url          = {http://dx.doi.org/10.1007/s12104-019-09879-w},
  year         = {2019},
}