Backbone


Journal

Biomolecular NMR assignments
ISSN: 1874-270X
Titre abrégé: Biomol NMR Assign
Pays: Netherlands
ID NLM: 101472371

Informations de publication

Date de publication:
04 2019
Historique:
received: 17 12 2018
accepted: 01 02 2019
pubmed: 9 2 2019
medline: 20 8 2019
entrez: 9 2 2019
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 30734154
doi: 10.1007/s12104-019-09879-w
pii: 10.1007/s12104-019-09879-w
pmc: PMC6439179
doi:

Substances chimiques

Carbon Isotopes 0
Nitrogen Isotopes 0
Nitrogen-15 0
Protons 0
beta-Mannosidase EC 3.2.1.25
Carbon-13 FDJ0A8596D

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Pagination

213-218

Références

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Auteurs

Sven Wernersson (S)

Department of Chemistry, Biophysical Chemistry, Center for Molecular Protein Science, Lund University, Lund, Sweden.

Viktoria Bågenholm (V)

Department of Chemistry, Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Lund, Sweden.

Cecilia Persson (C)

The Swedish NMR Center, University of Gothenburg, Gothenburg, Sweden.

Santosh Kumar Upadhyay (SK)

Department of Chemistry, Biophysical Chemistry, Center for Molecular Protein Science, Lund University, Lund, Sweden.

Henrik Stålbrand (H)

Department of Chemistry, Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Lund, Sweden.

Mikael Akke (M)

Department of Chemistry, Biophysical Chemistry, Center for Molecular Protein Science, Lund University, Lund, Sweden. mikael.akke@bpc.lu.se.

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