ArticleThe Journal of biological chemistry2014
Structure and substrate specificity of a eukaryotic fucosidase from Fusarium graminearum.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Structural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.The FEBS journal · 2025Article
- Article
- A Robust α-l-Fucosidase fromACS chemical biology · 2024Article
- Exploring the sequence-function space of microbial fucosidases.Communications chemistry · 2024Article
- Structure and function of microbial α-l-fucosidases: a mini review.Essays in biochemistry · 2023Review
- Machine learning prediction of novel pectinolytic enzymes inMicrobial genomics · 2021Article
- FRAGSITE: A Fragment-Based Approach for Virtual Ligand Screening.Journal of chemical information and modeling · 2021Article
- Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation.Nature communications · 2020Article
- Improved Transglycosylation by a Xyloglucan-Active α-l-Fucosidase fromJournal of fungi (Basel, Switzerland) · 2020Article
- Biochemical characterization of a novel α-L-fucosidase from Pedobacter sp. and its application in synthesis of 3'-fucosyllactose and 2'-fucosyllactose.Applied microbiology and biotechnology · 2020Article
- Crystal Structure of α-Xylosidase fromACS sustainable chemistry & engineering · 2020Article
- βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with CaJournal of bacteriology · 2019Article
- Adaptation of Syntenic Xyloglucan Utilization Loci of Human GutApplied and environmental microbiology · 2019Article
- FINDSITEJournal of chemical information and modeling · 2018Article
- An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.Glycobiology · 2018Article
- Identification and characterization of a core fucosidase from the bacteriumThe Journal of biological chemistry · 2018Article
- Genomic diversification of giant enteric symbionts reflects host dietary lifestyles.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Design of Artificial Glycosidases: Metallopeptides that Remove H Antigen from Human Erythrocytes.Angewandte Chemie (International ed. in English) · 2017Article
- Novel α-L-Fucosidases from a Soil Metagenome for Production of Fucosylated Human Milk Oligosaccharides.PloS one · 2016Article
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4 authors at 3 institutions in 1 country.
Funding
Abstract
The secreted glycoside hydrolase family 29 (GH29) α-L-fucosidase from plant pathogenic fungus Fusarium graminearum (FgFCO1) actively releases fucose from the xyloglucan fragment. We solved crystal structures of two active-site conformations, i.e. open and closed, of apoFgFCO1 and an open complex with product fucose at atomic resolution. The closed conformation supports catalysis by orienting the conserved general acid/base Glu-288 nearest the predicted glycosidic position, whereas the open conformation possibly represents an unreactive state with Glu-288 positioned away from the catalytic center. A flexible loop near the substrate binding site containing a non-conserved GGSFT sequence is ordered in the closed but not the open form. We also identified a novel C-terminal βγ-crystallin domain in FgFCO1 devoid of calcium binding motif whose homologous sequences are present in various glycoside hydrolase families. N-Glycosylated FgFCO1 adopts a monomeric state as verified by solution small angle x-ray scattering in contrast to reported multimeric fucosidases. Steady-state kinetics shows that FgFCO1 prefers α1,2 over α1,3/4 linkages and displays minimal activity with p-nitrophenyl fucoside with an acidic pH optimum of 4.6. Despite a retaining GH29 family fold, the overall specificity of FgFCO1 most closely resembles inverting GH95 α-fucosidase, which displays the highest specificity with two natural substrates harboring the Fucα1-2Gal glycosidic linkage, a xyloglucan-derived nonasaccharide, and 2'-fucosyllactose. Furthermore, FgFCO1 hydrolyzes H-disaccharide (lacking a +2 subsite sugar) at a rate 10(3)-fold slower than 2'-fucosyllactose. We demonstrated the structurally dynamic active site of FgFCO1 with flexible general acid/base Glu, a common feature shared by several bacterial GH29 fucosidases to various extents.
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