6NWZ
Crystal structure of Agd3 a novel carbohydrate deacetylase
Summary for 6NWZ
| Entry DOI | 10.2210/pdb6nwz/pdb |
| Descriptor | Carbohydrate deacetylase Agd3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | carbohydrate esterase, glycosylated, galactosaminogalactan de-n-acetylase, hydrolase |
| Biological source | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Total number of polymer chains | 1 |
| Total formula weight | 76213.18 |
| Authors | Bamford, N.C.,Howell, P.L. (deposition date: 2019-02-07, release date: 2020-02-12, Last modification date: 2024-11-13) |
| Primary citation | Bamford, N.C.,Le Mauff, F.,Van Loon, J.C.,Ostapska, H.,Snarr, B.D.,Zhang, Y.,Kitova, E.N.,Klassen, J.S.,Codee, J.D.C.,Sheppard, D.C.,Howell, P.L. Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation. Nat Commun, 11:2450-2450, 2020 Cited by PubMed Abstract: The exopolysaccharide galactosaminogalactan (GAG) is an important virulence factor of the fungal pathogen Aspergillus fumigatus. Deletion of a gene encoding a putative deacetylase, Agd3, leads to defects in GAG deacetylation, biofilm formation, and virulence. Here, we show that Agd3 deacetylates GAG in a metal-dependent manner, and is the founding member of carbohydrate esterase family CE18. The active site is formed by four catalytic motifs that are essential for activity. The structure of Agd3 includes an elongated substrate-binding cleft formed by a carbohydrate binding module (CBM) that is the founding member of CBM family 87. Agd3 homologues are encoded in previously unidentified putative bacterial exopolysaccharide biosynthetic operons and in other fungal genomes. PubMed: 32415073DOI: 10.1038/s41467-020-16144-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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