ArticleThe Journal of biological chemistry2010
Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo- and endo-type enzymes in glycoside hydrolase family 43.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 49 citations in OpenAlex.
- Complementary GH54 and GH43 α-L-Arabinofuranosidases fromJournal of applied glycoscience · 2026Article
- Functional and structural characterization of AtAbf43C: an exo-1,5-α-L-arabinofuranosidase from Acetivibrio thermocellus DSM1313.The Biochemical journal · 2025Article
- Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster ofInternational journal of molecular sciences · 2024Article
- Arabinan hydrolysis by GH43 enzymes of Hungateiclostridium clariflavum and the potential synergistic mechanisms.Applied microbiology and biotechnology · 2022Article
- Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase.Communications biology · 2022Article
- Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting α-L-Arabinofuranosidase Activity.Frontiers in molecular biosciences · 2022Article
- The Role of Arabinogalactan Type II Degradation in Plant-Microbe Interactions.Frontiers in microbiology · 2021Review
- The PhoPQ Two-Component System Is the Major Regulator of Cell Surface Properties, Stress Responses and Plant-Derived Substrate Utilisation During Development ofFrontiers in microbiology · 2020Article
- Two Novel α-l-Arabinofuranosidases fromApplied and environmental microbiology · 2019Article
- Structural dissection of a complex Bacteroides ovatus gene locus conferring xyloglucan metabolism in the human gut.Open biology · 2016Article
- Functional and structural diversity in GH62 α-L-arabinofuranosidases from the thermophilic fungus Scytalidium thermophilum.Microbial biotechnology · 2015Article
- High-resolution crystal structure of a polyextreme GH43 glycosidase from Halothermothrix orenii with α-L-arabinofuranosidase activity.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.The Journal of biological chemistry · 2014Article
- Mechanistic strategies for catalysis adopted by evolutionary distinct family 43 arabinanases.The Journal of biological chemistry · 2014Article
- Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, β-1,4-mannooligosaccharide phosphorylase.The Journal of biological chemistry · 2012Article
- Introducing endo-xylanase activity into an exo-acting arabinofuranosidase that targets side chains.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases.The Journal of biological chemistry · 2011Article
- Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 α-glucuronidase from Streptomyces pristinaespiralis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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6 authors at 2 institutions in 1 country.
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Abstract
Exo-1,5-α-L-arabinofuranosidases belonging to glycoside hydrolase family 43 have strict substrate specificity. These enzymes hydrolyze only the α-1,5-linkages of linear arabinan and arabino-oligosaccharides in an exo-acting manner. The enzyme from Streptomyces avermitilis contains a core catalytic domain belonging to glycoside hydrolase family 43 and a C-terminal arabinan binding module belonging to carbohydrate binding module family 42. We determined the crystal structure of intact exo-1,5-α-L-arabinofuranosidase. The catalytic module is composed of a 5-bladed β-propeller topologically identical to the other family 43 enzymes. The arabinan binding module had three similar subdomains assembled against one another around a pseudo-3-fold axis, forming a β-trefoil-fold. A sugar complex structure with α-1,5-L-arabinofuranotriose revealed three subsites in the catalytic domain, and a sugar complex structure with α-L-arabinofuranosyl azide revealed three arabinose-binding sites in the carbohydrate binding module. A mutagenesis study revealed that substrate specificity was regulated by residues Asn-159, Tyr-192, and Leu-289 located at the aglycon side of the substrate-binding pocket. The exo-acting manner of the enzyme was attributed to the strict pocket structure of subsite -1, formed by the flexible loop region Tyr-281-Arg-294 and the side chain of Tyr-40, which occupied the positions corresponding to the catalytic glycon cleft of GH43 endo-acting enzymes.
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