ArticleScientific reports2019
First crystal structure of an endo-levanase - the BT1760 from a human gut commensal Bacteroides thetaiotaomicron.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
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11 citing papers in PubMed, 33 citations in OpenAlex.
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- A Refined Nomenclature System to Better Discriminate Endo- and Exo-Type Fructanases and Glucanases.Biomolecules · 2024Article
- Frequent Acquisition of Glycoside Hydrolase Family 32 (GH32) Genes from Bacteria via Horizontal Gene Transfer Drives Adaptation of Invertebrates to Diverse Sources of Food and Living Habitats.International journal of molecular sciences · 2024Article
- Iron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection.Cell host & microbe · 2023Article
- Article
- Single-molecule dynamics of surface lipoproteins in bacteroides indicate similarities and cooperativity.Biophysical journal · 2022Article
- Functional Characterization of Recombinant Endo-Levanase (LevBk) from Bacillus koreensis HL12 on Short-Chain Levan-Type Fructooligosaccharides Production.The protein journal · 2022Article
- Enzymatic and structural characterization of β-fructofuranosidase from the honeybee gut bacterium Frischella perrara.Applied microbiology and biotechnology · 2022Article
- Insights into SusCD-mediated glycan import by a prominent gut symbiont.Nature communications · 2021Article
- Characterization of a Maltase from an Early-Diverged Non-Conventional YeastInternational journal of molecular sciences · 2019Article
- Diversity and Function of Phage Encoded Depolymerases.Frontiers in microbiology · 2019Review
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The endo-levanase BT1760 of a human gut commensal Bacteroides thetaiotaomicron randomly cuts a β-2,6-linked fructan, levan, into fructo-oligosaccharides providing a prebiotic substrate for gut microbiota. Here we introduce the crystal structure of BT1760 at resolution of 1.65 Å. The fold of the enzyme is typical for GH32 family proteins: a catalytic N-terminal five-bladed β-propeller connected with a C-terminal β-sandwich domain. The levantetraose-bound structure of catalytically inactive mutant E221A at 1.90-Å resolution reveals differences in substrate binding between the endo-acting fructanases. A shallow substrate-binding pocket of the endo-inulinase INU2 of Aspergillus ficuum binds at least three fructose residues at its flat bottom. In the levantetraose-soaked crystal of the endo-levanase E221A mutant the ligand was bent into the pond-like substrate pocket with its fructose residues making contacts at -3, -2, -1 and + 1 subsites residing at several pocket depths. Binding of levantetraose to the β-sandwich domain was not detected. The N- and C-terminal modules of BT1760 did not bind levan if expressed separately, the catalytic domain lost its activity and both modules tended to precipitate. We gather that endo-levanase BT1760 requires both domains for correct folding, solubility and stability of the protein.
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