9LXL
Crystal structure of GH29 family alpha-L-fucosidase from Fusarium proliferatum LE1
Summary for 9LXL
| Entry DOI | 10.2210/pdb9lxl/pdb |
| Descriptor | alpha-L-fucosidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (8 entities in total) |
| Functional Keywords | alpha-l-fucosidase, gh29, fusarium proliferatum, hydrolase |
| Biological source | Gibberella intermedia (Bulb rot disease fungus, Fusarium proliferatum) |
| Total number of polymer chains | 1 |
| Total formula weight | 70470.87 |
| Authors | Korban, S.A.,Borshchevskiy, V.I.,Pospelov, V.A.,Bobrov, K.S.,Ivanova, D.N.,Kulminskaya, A.A. (deposition date: 2025-02-18, release date: 2025-03-19, Last modification date: 2025-08-27) |
| Primary citation | Korban, S.,Bobrov, K.,Borshchevskiy, V.,Pospelov, V.,Shvetsov, A.,Titov, A.,Eneyskaya, E.,Kulminskaya, A. Structure and biochemical characterization of GH29 family alpha-l-fucosidase from Fusarium proliferatum LE1. Biochem.Biophys.Res.Commun., 779:152451-152451, 2025 Cited by PubMed Abstract: Alpha-L-fucosidases are essential tools for studying the structure-function relationships of fucosylated sugars and for the synthesis of glycoconjugates. Despite their significant potential in biotechnology, detailed structural and mechanistic aspects of these enzymes remain poorly understood. In this study, we identified a novel α-l-fucosidase from the fungus Fusarium proliferatum LE1, belonging to the GH29 family of glycoside hydrolases. The recombinant protein was purified and biochemically characterized. The crystal structure of the enzyme was determined at anisotropic resolution of 2.2-2.6 Å in the closed conformation of the active site. Structural comparison with homologous proteins revealed a conserved catalytic domain and a non-conserved C-terminal domain, which displays significant flexibility in the crystal, as confirmed by molecular dynamics simulations. We propose that this flexibility reflects intrinsic enzyme dynamics, enabling substrate recognition, binding, and translocation to the active site. PubMed: 40782452DOI: 10.1016/j.bbrc.2025.152451 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.191 Å) |
Structure validation
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