ArticleThe Journal of biological chemistry2010
Structural insights into the specificity of Xyn10B from Paenibacillus barcinonensis and its improved stability by forced protein evolution.
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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Who cites it
18 citing papers in PubMed, 53 citations in OpenAlex.
- Endo-β-1,4-Xylanase GH10 fromInternational journal of molecular sciences · 2026Article
- Detection of the Microbial Composition of Some Commercial Fermented Liquid Products via Metagenomic Analysis.Foods (Basel, Switzerland) · 2023Article
- Selection signature analysis revealsArchives animal breeding · 2023Article
- Thermostability modification of β-mannanase fromFrontiers in microbiology · 2023Article
- Contribution of the mutation rs8193069 in TLR4 to mastitis resistance and performance in Holstein cows in southern China.Veterinary medicine and science · 2022Article
- Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity.Computational and structural biotechnology journal · 2021Article
- Microbial Cell Factory of Baccatin III Preparation inFrontiers in microbiology · 2021Article
- 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
- Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis.Scientific reports · 2016Article
- Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives.World journal of microbiology & biotechnology · 2016Review
- 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
- Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.The Journal of biological chemistry · 2014Article
- Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity.The Journal of biological chemistry · 2014Article
- A thermo-halo-tolerant and proteinase-resistant endoxylanase from Bacillus sp. HJ14.Folia microbiologica · 2014Article
- Enhanced enzyme kinetic stability by increasing rigidity within the active site.The Journal of biological chemistry · 2014Article
- Biochemical characterization of two thermostable xylanolytic enzymes encoded by a gene cluster of Caldicellulosiruptor owensensis.PloS one · 2014Article
- Modular glucuronoxylan-specific xylanase with a family CBM35 carbohydrate-binding module.Applied and environmental microbiology · 2012Article
- Characterization of a family GH5 xylanase with activity on neutral oligosaccharides and evaluation as a pulp bleaching aid.Applied and environmental microbiology · 2010Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paenibacillus barcinonensis is a soil bacterium bearing a complex set of enzymes for xylan degradation, including several secreted enzymes and Xyn10B, one of the few intracellular xylanases reported to date. The crystal structure of Xyn10B has been determined by x-ray analysis. The enzyme folds into the typical (beta/alpha)(8) barrel of family 10 glycosyl hydrolases (GH10), with additional secondary structure elements within the beta/alpha motifs. One of these loops -L7- located at the beta7 C terminus, was essential for xylanase activity as its partial deletion yielded an inactive enzyme. The loop contains residues His(249)-Glu(250), which shape a pocket opened to solvent in close proximity to the +2 subsite, which has not been described in other GH10 enzymes. This wide cavity at the +2 subsite, where methyl-2,4-pentanediol from the crystallization medium was found, is a noteworthy feature of Xyn10B, as compared with the narrow crevice described for other GH10 xylanases. Docking analysis showed that this open cavity can accommodate glucuronic acid decorations of xylo-oligosaccharides. Co-crystallization experiments with conduramine derivative inhibitors supported the importance of this open cavity at the +2 subsite for Xyn10B activity. Several mutant derivatives of Xyn10B with improved thermal stability were obtained by forced evolution. Among them, mutant xylanases S15L and M93V showed increased half-life, whereas the double mutant S15L/M93V exhibited a further increase in stability, showing a 20-fold higher heat resistance than the wild type xylanase. All the mutations obtained were located on the surface of Xyn10B. Replacement of a Ser by a Leu residue in mutant xylanase S15L can increase hydrophobic packing efficiency and fill a superficial indentation of the protein, giving rise to a more compact structure of the enzyme.
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