ArticleThe Journal of biological chemistry2014
Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity.
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 18 papers.
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18 citing papers in PubMed, 52 citations in OpenAlex.
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- Direct Phasing of Protein Crystals with Continuous Iterative Projection Algorithms and Refined Envelope Reconstruction.Biomolecules · 2026Article
- A Synthetic Lectin for Glucuronate.ACS central science · 2025Article
- Comprehensive Genome Analysis of Cellulose and Xylan-Active CAZymes from the GenusMicrobiology spectrum · 2023Article
- Functional identification of two novel carbohydrate-binding modules of glucuronoxylanase CrXyl30 and their contribution to the lignocellulose saccharification.Biotechnology for biofuels and bioproducts · 2023Article
- The structure of aJournal of structural biology: X · 2023Article
- Novel Nematode-Killing Protein-1 (Nkp-1) from a Marine Epiphytic BacteriumBiomedicines · 2021Article
- Friend or Foe? Impacts of Dietary Xylans, Xylooligosaccharides, and Xylanases on Intestinal Health and Growth Performance of Monogastric Animals.Animals : an open access journal from MDPI · 2021Review
- A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum.Applied microbiology and biotechnology · 2021Article
- A New Subfamily of Glycoside Hydrolase Family 30 with Strict Xylobiohydrolase Function.Frontiers in molecular biosciences · 2021Article
- A novel fungal GH30 xylanase with xylobiohydrolase auxiliary activity.Biotechnology for biofuels · 2019Article
- Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.Applied microbiology and biotechnology · 2018Review
- Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation.Extremophiles : life under extreme conditions · 2018Review
- Structural Considerations on the Use of Endo-Xylanases for the Production of prebiotic Xylooligosaccharides from Biomass.Current protein & peptide science · 2018Review
- Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates.The Journal of biological chemistry · 2017Article
- Diverse modes of galacto-specific carbohydrate recognition by a family 31 glycoside hydrolase from Clostridium perfringens.PloS one · 2017Article
- The Glycoside Hydrolase Family 8 Reducing-End Xylose-Releasing Exo-oligoxylanase Rex8A from Paenibacillus barcinonensis BP-23 Is Active on Branched Xylooligosaccharides.Applied and environmental microbiology · 2016Article
- Exploring Multimodularity in Plant Cell Wall Deconstruction: STRUCTURAL AND FUNCTIONAL ANALYSIS OF Xyn10C CONTAINING THE CBM22-1-CBM22-2 TANDEM.The Journal of biological chemistry · 2015Article
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5 authors at 1 institution in 1 country.
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Abstract
Glucuronoxylanase Xyn30D is a modular enzyme containing a family 30 glycoside hydrolase catalytic domain and an attached carbohydrate binding module of the CBM35 family. We present here the three-dimensional structure of the full-length Xyn30D at 2.4 Å resolution. The catalytic domain folds into an (α/β)8 barrel with an associated β-structure, whereas the attached CBM35 displays a jellyroll β-sandwich including two calcium ions. Although both domains fold in an independent manner, the linker region makes polar interactions with the catalytic domain, allowing a moderate flexibility. The ancillary Xyn30D-CBM35 domain has been expressed and crystallized, and its binding abilities have been investigated by soaking experiments. Only glucuronic acid-containing ligands produced complexes, and their structures have been solved. A calcium-dependent glucuronic acid binding site shows distinctive structural features as compared with other uronic acid-specific CBM35s, because the presence of two aromatic residues delineates a wider pocket. The nonconserved Glu(129) makes a bidentate link to calcium and defines region E, previously identified as specificity hot spot. The molecular surface of Xyn30D-CBM35 shows a unique stretch of negative charge distribution extending from its binding pocket that might indicate some oriented interaction with its target substrate. The binding ability of Xyn30D-CBM35 to different xylans was analyzed by affinity gel electrophoresis. Some binding was observed with rye glucuronoarabinoxylan in presence of calcium chelating EDTA, which would indicate that Xyn30D-CBM35 might establish interaction to other components of xylan, such as arabinose decorations of glucuronoarabinoxylan. A role in depolymerization of highly substituted chemically complex xylans is proposed.
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