ArticleNature communications2024
Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- EgSPE, a secreted protein from Epichloë gansuensis, modulates symbiotic establishment and host drought tolerance.BMC plant biology · 2026Article
- Alginate oligosaccharides in the food industry: emerging functional roles, health benefits, and technological applications - Review.Food chemistry: X · 2025Review
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Genome-wide identification and biochemical characterization of glycoside hydrolase gene family members in Tilletia Horrida.Molecular biology reports · 2024Article
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14 authors.
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Abstract
Carbohydrate-binding modules (CBMs) are non-catalytic proteins found appended to carbohydrate-active enzymes. Soil and marine bacteria secrete such enzymes to scavenge nutrition, and they often use CBMs to improve reaction rates and retention of released sugars. Here we present a structural and functional analysis of the recently established CBM family 92. All proteins analysed bind preferentially to β-1,6-glucans. This contrasts with the diversity of predicted substrates among the enzymes attached to CBM92 domains. We present crystal structures for two proteins, and confirm by mutagenesis that tryptophan residues permit ligand binding at three distinct functional binding sites on each protein. Multivalent CBM families are uncommon, so the establishment and structural characterisation of CBM92 enriches the classification database and will facilitate functional prediction in future projects. We propose that CBM92 proteins may cross-link polysaccharides in nature, and might have use in novel strategies for enzyme immobilisation.
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