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Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family
- Source :
- Nature chemical biology. 16(8)
- Publication Year :
- 2019
-
Abstract
- 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.
Details
- ISSN :
- 15524469
- Volume :
- 16
- Issue :
- 8
- Database :
- OpenAIRE
- Journal :
- Nature chemical biology
- Accession number :
- edsair.pmid..........de179a9161d83e217bed02a213c39aa2