ArticleActa crystallographica. Section F, Structural biology communications2016
The structure of a glycoside hydrolase 29 family member from a rumen bacterium reveals unique, dual carbohydrate-binding domains.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 19 citations in OpenAlex.
- Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities.Nature communications · 2025Article
- Mechanism of 2'-fucosyllactose degradation by human-associatedJournal of bacteriology · 2024Article
- Biochemical characterization of Fsa16295Glu fromFrontiers in microbiology · 2024Article
- Structure and function of microbial α-l-fucosidases: a mini review.Essays in biochemistry · 2023Review
- Article
- Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation.Nature communications · 2020Article
- Functional exploration of the GH29 fucosidase family.Glycobiology · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycoside hydrolase (GH) family 29 consists solely of α-L-fucosidases. These enzymes catalyse the hydrolysis of glycosidic bonds. Here, the structure of GH29_0940, a protein cloned from metagenomic DNA from the rumen of a cow, has been solved, which reveals a multi-domain arrangement that has only recently been identified in bacterial GH29 enzymes. The microbial species that provided the source of this enzyme is unknown. This enzyme contains a second carbohydrate-binding domain at its C-terminal end in addition to the typical N-terminal catalytic domain and carbohydrate-binding domain arrangement of GH29-family proteins. GH29_0940 is a monomer and its overall structure consists of an N-terminal TIM-barrel-like domain, a central β-sandwich domain and a C-terminal β-sandwich domain. The TIM-barrel-like catalytic domain exhibits a (β/α)
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