Результаты исследований: Научные публикации в периодических изданиях › статья
Structure and biochemical characterization of GH29 family α-L-fucosidase from Fusarium proliferatum LE1. / Корбан, Светлана Андреевна; Бобров, К.С.; Borshchevskiy, Valentin I.; Pospelov, VA; Shvetsov, Alexey V.; Titov, A.; Eneyskaya, E.V.; Kulminskaya, Anna A.
в: Biochemical and Biophysical Research Communications, Том 779, 152451, 12.09.2025.Результаты исследований: Научные публикации в периодических изданиях › статья
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TY - JOUR
T1 - Structure and biochemical characterization of GH29 family α-L-fucosidase from Fusarium proliferatum LE1
AU - Корбан, Светлана Андреевна
AU - Бобров, К.С.
AU - Borshchevskiy, Valentin I.
AU - Pospelov, VA
AU - Shvetsov, Alexey V.
AU - Titov, A.
AU - Eneyskaya, E.V.
AU - Kulminskaya, Anna A.
PY - 2025/9/12
Y1 - 2025/9/12
N2 - 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.
AB - 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.
KW - Alpha-L-fucosidase
KW - Crystal structure
KW - Fusarium proliferatum
KW - GH29 family
KW - βγ-crystallin domain
KW - Amino Acid Sequence
KW - Catalytic Domain
KW - alpha-L-Fucosidase/chemistry
KW - Substrate Specificity
KW - Crystallography, X-Ray
KW - Molecular Dynamics Simulation
KW - Recombinant Proteins/chemistry
KW - Fungal Proteins/chemistry
KW - Fusarium/enzymology
KW - Protein Conformation
UR - https://www.mendeley.com/catalogue/e93e2e8c-304e-345e-ab6a-e41d147f772d/
U2 - 10.1016/j.bbrc.2025.152451
DO - 10.1016/j.bbrc.2025.152451
M3 - Article
C2 - 40782452
VL - 779
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
M1 - 152451
ER -
ID: 140083303