ArticleActa crystallographica. Section D, Structural biology2022
Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.
Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Non-Catalytic Domains of Glycoside Hydrolase Family 5 fromJournal of microbiology and biotechnology · 2025Article
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Important roles ofFood science and biotechnology · 2024Review
- Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024Article
- Ephedra sinica polysaccharide regulate the anti-inflammatory immunity of intestinal microecology and bacterial metabolites in rheumatoid arthritis.Frontiers in pharmacology · 2024Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most known cellulase-associated carbohydrate-binding modules (CBMs) are attached to the N- or C-terminus of the enzyme or are expressed separately and assembled into multi-enzyme complexes (for example to form cellulosomes), rather than being an insertion into the catalytic domain. Here, by solving the crystal structure, it is shown that MtGlu5 from Meiothermus taiwanensis WR-220, a GH5-family endo-β-1,4-glucanase (EC 3.2.1.4), has a bipartite architecture consisting of a Cel5A-like catalytic domain with a (β/α)
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