Fig. 4: Agd3 deacetylates GAG in a metal-dependent manner. | Nature Communications

Fig. 4: Agd3 deacetylates GAG in a metal-dependent manner.

From: Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation

Fig. 4

a Cartoon representation of the conserved active site residues including the metal coordinating triad (yellow), the putative catalytic base (green), and the putative catalytic acid (pink). b Absorbance of crystal violet stained 21 h old biofilms of Δagd3 or WT strains after treatment as labeled. Bars indicate mean ± SD and represent three independent experiments of n = 6. Representative stained biofilms in a 96-well plate are aligned below. c Agd3 deacetylation of GAG as measured by the GAG-ELLA. The experiment was run in triplicate. d Agd3 deacetylates GAG in a metal-dependent mechanism. Each condition had a total number of n = 21 for all metal conditions except Ni2+ with n = 9, n = 34 for as isolated, n = 12 for EDTA, and n = 28 for DPA, representing individual wells spread over nine independent experiments. e Metal-dependent de-N-acetylation reaction based on the findings of the activity assays and CE4 enzymes. The residues are color coded as in a. For b and d statistics were calculated one-way ANOVA with Dunnett’s multiple comparison test. *p < 0.033, ***p < 0.0002, ****p < 0.0001. Error bars represent SD. Source data is available in Source Data file.

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