ArticleThe Journal of biological chemistry2016
The Mechanism by Which Arabinoxylanases Can Recognize Highly Decorated Xylans.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A chemoproteomic biotechnological toolkit for resolving xylanase specificity in decorated xylan.Nature communications · 2026Article
- Structural insights into a fucosidase involved in fucoidan degradation.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- Functional studies on tandem carbohydrate-binding modules of a multimodular enzyme possessing two catalytic domains.Applied and environmental microbiology · 2024Article
- Inter domain linker region affects properties of CBM6 in GH5_34 arabinoxylanases and alters oligosaccharide product profile.Glycobiology · 2024Article
- Novel thermostable GH5_34 arabinoxylanase with an atypical CBM6 displays activity on oat fiber xylan for prebiotic production.Glycobiology · 2023Article
- Three marine species of the genus Fulvivirga, rich sources of carbohydrate-active enzymes degrading alginate, chitin, laminarin, starch, and xylan.Scientific reports · 2023Article
- Grass xylan structural variation suggests functional specialization and distinctive interaction with cellulose and lignin.The Plant journal : for cell and molecular biology · 2023Article
- Novel Function of CtXyn5A from Acetivibrio thermocellus: Dual Arabinoxylanase and Feruloyl Esterase Activity in the Same Active Site.Chembiochem : a European journal of chemical biology · 2023Article
- The first crystal structure of a xylobiose-bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10.FEBS letters · 2022Article
- Recent advances in the enzymatic production and applications of xylooligosaccharides.World journal of microbiology & biotechnology · 2021Review
- Non-Specific GH30_7 Endo-β-1,4-xylanase fromMolecules (Basel, Switzerland) · 2021Article
- Carbohydrate-binding modules targeting branched polysaccharides: overcoming side-chain recalcitrance in a non-catalytic approach.Bioresources and bioprocessing · 2021Review
- Biochemical analysis of cross-feeding behaviour between two common gut commensals when cultivated on plant-derived arabinogalactan.Microbial biotechnology · 2020Article
- Verrucomicrobia use hundreds of enzymes to digest the algal polysaccharide fucoidan.Nature microbiology · 2020Article
- Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.Applied microbiology and biotechnology · 2018Review
- SACCHARIS: an automated pipeline to streamline discovery of carbohydrate active enzyme activities within polyspecific families and de novo sequence datasets.Biotechnology for biofuels · 2018Article
- Dynamic changes in transcriptome and cell wall composition underlying brassinosteroid-mediated lignification of switchgrass suspension cells.Biotechnology for biofuels · 2017Article
- Structure-dependent stimulation of gut bacteria by arabinoxylo-oligosaccharides (AXOS): a review.Gut microbesReview
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Authors and funding
13 authors.
Funding
Abstract
The enzymatic degradation of plant cell walls is an important biological process of increasing environmental and industrial significance. Xylan, a major component of the plant cell wall, consists of a backbone of β-1,4-xylose (Xylp) units that are often decorated with arabinofuranose (Araf) side chains. A large penta-modular enzyme, CtXyl5A, was shown previously to specifically target arabinoxylans. The mechanism of substrate recognition displayed by the enzyme, however, remains unclear. Here we report the crystal structure of the arabinoxylanase and the enzyme in complex with ligands. The data showed that four of the protein modules adopt a rigid structure, which stabilizes the catalytic domain. The C-terminal non-catalytic carbohydrate binding module could not be observed in the crystal structure, suggesting positional flexibility. The structure of the enzyme in complex with Xylp-β-1,4-Xylp-β-1,4-Xylp-[α-1,3-Araf]-β-1,4-Xylp showed that the Araf decoration linked O
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