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The fundamental and assorted roles of β-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. In this work, the selectivity and modes of action of a glycoside hydrolase family active on β-1,3-glucans were systematically investigated combining sequence similarity network, phylogeny, X-ray crystallography, enzyme kinetics, mutagenesis and molecular dynamics. This family exhibits a minimalist and versatile (α/β)-barrel scaffold, which can harbor distinguishing exo or endo modes of action, including an ancillary-binding site for the anchoring of triple-helical β-1,3-glucans. The substrate binding occurs via a hydrophobic knuckle complementary to the canonical curved conformation of β-1,3-glucans or through a substrate conformational change imposed by the active-site topology of some fungal enzymes. Together, these findings expand our understanding of the enzymatic arsenal of bacteria and fungi for the breakdown and modification of β-1,3-glucans, which can be exploited for biotechnological applications.


Camila R Santos, Pedro A C R Costa, Plínio S Vieira, Sinkler E T Gonzalez, Thamy L R Correa, Evandro A Lima, Fernanda Mandelli, Renan A S Pirolla, Mariane N Domingues, Lucelia Cabral, Marcele P Martins, Rosa L Cordeiro, Atílio T Junior, Beatriz P Souza, Érica T Prates, Fabio C Gozzo, Gabriela F Persinoti, Munir S Skaf, Mario T Murakami. Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family. Nature chemical biology. 2020 Aug;16(8):920-929

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PMID: 32451508

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