ArticleThe Journal of biological chemistry2011
Structure and function of an arabinoxylan-specific xylanase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 109 citations in OpenAlex.
- A chemoproteomic biotechnological toolkit for resolving xylanase specificity in decorated xylan.Nature communications · 2026Article
- Expression and characterization of an endo-β-1,6-galactanase from Arabidopsis thaliana.The Biochemical journal · 2025Article
- Structural insights into a fucosidase involved in fucoidan degradation.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Inter domain linker region affects properties of CBM6 in GH5_34 arabinoxylanases and alters oligosaccharide product profile.Glycobiology · 2024Article
- Enhancing Mechanical Properties of Corn Bran Arabinoxylan Films for Sustainable Food Packaging.Foods (Basel, Switzerland) · 2024Article
- Novel thermostable GH5_34 arabinoxylanase with an atypical CBM6 displays activity on oat fiber xylan for prebiotic production.Glycobiology · 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
- Genome-Wide Association Study of Arabinoxylan Content from a 562 Hexaploid Wheat Collection.Plants (Basel, Switzerland) · 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
- Generation of a Library of Carbohydrate-Active Enzymes for Plant Biomass Deconstruction.International journal of molecular sciences · 2022Article
- Recent advances in the enzymatic production and applications of xylooligosaccharides.World journal of microbiology & biotechnology · 2021Review
- Novel 3-Applied and environmental microbiology · 2021Article
- Degradation profile of nixtamalized maize pericarp by the action of the microbial consortium PM-06.AMB Express · 2019Article
- Molecular Basis of Broad SpectrumACS central science · 2019Article
- Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.Applied microbiology and biotechnology · 2018Review
- A bifunctional cellulase-xylanase of a new Chryseobacterium strain isolated from the dung of a straw-fed cattle.Microbial biotechnology · 2018Article
- Molecular structure and catalytic mechanism of fungal family G acidophilic xylanases.3 Biotech · 2018Review
- Structural Considerations on the Use of Endo-Xylanases for the Production of prebiotic Xylooligosaccharides from Biomass.Current protein & peptide science · 2018Review
- Structural Insights into the Broad Substrate Specificity of a Novel Endoglycoceramidase I Belonging to a New Subfamily of GH5 Glycosidases.The Journal of biological chemistry · 2017Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymatic degradation of plant cell walls plays a central role in the carbon cycle and is of increasing environmental and industrial significance. The enzymes that catalyze this process include xylanases that degrade xylan, a β-1,4-xylose polymer that is decorated with various sugars. Although xylanases efficiently hydrolyze unsubstituted xylans, these enzymes are unable to access highly decorated forms of the polysaccharide, such as arabinoxylans that contain arabinofuranose decorations. Here, we show that a Clostridium thermocellum enzyme, designated CtXyl5A, hydrolyzes arabinoxylans but does not attack unsubstituted xylans. Analysis of the reaction products generated by CtXyl5A showed that all the oligosaccharides contain an O3 arabinose linked to the reducing end xylose. The crystal structure of the catalytic module (CtGH5) of CtXyl5A, appended to a family 6 noncatalytic carbohydrate-binding module (CtCBM6), showed that CtGH5 displays a canonical (α/β)(8)-barrel fold with the substrate binding cleft running along the surface of the protein. The catalytic apparatus is housed in the center of the cleft. Adjacent to the -1 subsite is a pocket that could accommodate an l-arabinofuranose-linked α-1,3 to the active site xylose, which is likely to function as a key specificity determinant. CtCBM6, which adopts a β-sandwich fold, recognizes the termini of xylo- and gluco-configured oligosaccharides, consistent with the pocket topology displayed by the ligand-binding site. In contrast to typical modular glycoside hydrolases, there is an extensive hydrophobic interface between CtGH5 and CtCBM6, and thus the two modules cannot function as independent entities.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.