| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-120 |
Sentence |
denotes |
Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms. |
| T2 |
121-234 |
Sentence |
denotes |
Aspergillus fumigatus is an opportunistic fungal pathogen that causes both chronic and acute invasive infections. |
| T3 |
235-350 |
Sentence |
denotes |
Galactosaminogalactan (GAG) is an integral component of the A. fumigatus biofilm matrix and a key virulence factor. |
| T4 |
351-483 |
Sentence |
denotes |
GAG is a heterogeneous linear α-1,4-linked exopolysaccharide of galactose and GalNAc that is partially deacetylated after secretion. |
| T5 |
484-574 |
Sentence |
denotes |
A cluster of five co-expressed genes has been linked to GAG biosynthesis and modification. |
| T6 |
575-719 |
Sentence |
denotes |
One gene in this cluster, ega3, is annotated as encoding a putative α-1,4-galactosaminidase belonging to glycoside hydrolase family 114 (GH114). |
| T7 |
720-925 |
Sentence |
denotes |
Herein, we show that recombinant Ega3 is an active glycoside hydrolase that disrupts GAG-dependent A. fumigatus and Pel polysaccharide-dependent Pseudomonas aeruginosa biofilms at nanomolar concentrations. |
| T8 |
926-1102 |
Sentence |
denotes |
Using MS and functional assays, we demonstrate that Ega3 is an endo-acting α-1,4-galactosaminidase whose activity depends on the conserved acidic residues, Asp-189 and Glu-247. |
| T9 |
1103-1349 |
Sentence |
denotes |
X-ray crystallographic structural analysis of the apo Ega3 and an Ega3-galactosamine complex, at 1.76 and 2.09 Å resolutions, revealed a modified (β/α)8-fold with a deep electronegative cleft, which upon ligand binding is capped to form a tunnel. |
| T10 |
1350-1540 |
Sentence |
denotes |
Our structural analysis coupled with in silico docking studies also uncovered the molecular determinants for galactosamine specificity and substrate binding at the -2 to +1 binding subsites. |
| T11 |
1541-1769 |
Sentence |
denotes |
The findings in this study increase the structural and mechanistic understanding of the GH114 family, which has >600 members encoded by plant and opportunistic human pathogens, as well as in industrially used bacteria and fungi. |
| T1 |
0-120 |
Sentence |
denotes |
Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms. |
| T2 |
121-234 |
Sentence |
denotes |
Aspergillus fumigatus is an opportunistic fungal pathogen that causes both chronic and acute invasive infections. |
| T3 |
235-350 |
Sentence |
denotes |
Galactosaminogalactan (GAG) is an integral component of the A. fumigatus biofilm matrix and a key virulence factor. |
| T4 |
351-483 |
Sentence |
denotes |
GAG is a heterogeneous linear α-1,4-linked exopolysaccharide of galactose and GalNAc that is partially deacetylated after secretion. |
| T5 |
484-574 |
Sentence |
denotes |
A cluster of five co-expressed genes has been linked to GAG biosynthesis and modification. |
| T6 |
575-719 |
Sentence |
denotes |
One gene in this cluster, ega3, is annotated as encoding a putative α-1,4-galactosaminidase belonging to glycoside hydrolase family 114 (GH114). |
| T7 |
720-925 |
Sentence |
denotes |
Herein, we show that recombinant Ega3 is an active glycoside hydrolase that disrupts GAG-dependent A. fumigatus and Pel polysaccharide-dependent Pseudomonas aeruginosa biofilms at nanomolar concentrations. |
| T8 |
926-1102 |
Sentence |
denotes |
Using MS and functional assays, we demonstrate that Ega3 is an endo-acting α-1,4-galactosaminidase whose activity depends on the conserved acidic residues, Asp-189 and Glu-247. |
| T9 |
1103-1349 |
Sentence |
denotes |
X-ray crystallographic structural analysis of the apo Ega3 and an Ega3-galactosamine complex, at 1.76 and 2.09 Å resolutions, revealed a modified (β/α)8-fold with a deep electronegative cleft, which upon ligand binding is capped to form a tunnel. |
| T10 |
1350-1540 |
Sentence |
denotes |
Our structural analysis coupled with in silico docking studies also uncovered the molecular determinants for galactosamine specificity and substrate binding at the -2 to +1 binding subsites. |
| T11 |
1541-1769 |
Sentence |
denotes |
The findings in this study increase the structural and mechanistic understanding of the GH114 family, which has >600 members encoded by plant and opportunistic human pathogens, as well as in industrially used bacteria and fungi. |