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- Title
Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans.
- Authors
Hao, Meng-Shu; Mazurkewich, Scott; Li, He; Kvammen, Alma; Saha, Srijani; Koskela, Salla; Inman, Annie R.; Nakajima, Masahiro; Tanaka, Nobukiyo; Nakai, Hiroyuki; Brändén, Gisela; Bulone, Vincent; Larsbrink, Johan; McKee, Lauren S.
- 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. Carbohydrate binding modules (CBMs) are non-catalytic domains found within multi-modular carbohydrate-active enzymes like glycoside hydrolases. Here, the authors show the crystal structures of two CBM family 92 members, which use three different surface binding sites to bind to β-glucans.
- Subjects
BACTERIAL enzymes; GLYCOSIDASES; BINDING sites; LIGAND binding (Biochemistry); MARINE bacteria; TRYPTOPHAN
- Publication
Nature Communications, 2024, Vol 15, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-024-47584-y