Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans

Meng-Shu Hao, Scott Mazurkewich, He Li, Alma Kvammen, Srijani Saha, Salla Koskela, Annie R. Inman, Masahiro Nakajima, Nobukiyo Tanaka, Hiroyuki Nakai, Gisela Brändén, Vincent Bulone, Johan Larsbrink and Lauren S. McKee ()
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Meng-Shu Hao: AlbaNova University Centre
Scott Mazurkewich: Chalmers University of Technology
He Li: AlbaNova University Centre
Alma Kvammen: AlbaNova University Centre
Srijani Saha: AlbaNova University Centre
Salla Koskela: AlbaNova University Centre
Annie R. Inman: AlbaNova University Centre
Masahiro Nakajima: Tokyo University of Science
Nobukiyo Tanaka: Tokyo University of Science
Hiroyuki Nakai: Niigata University
Gisela Brändén: University of Gothenburg
Vincent Bulone: AlbaNova University Centre
Johan Larsbrink: Chalmers University of Technology
Lauren S. McKee: AlbaNova University Centre

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-47584-y

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