ArticleProtein science : a publication of the Protein Society2011
Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- The In Silico Characterization of Monocotyledonous α-l-Arabinofuranosidases on the Example of Maize.Life (Basel, Switzerland) · 2023Article
- Two Subgroups within the GH43_36 α-l-Arabinofuranosidase Subfamily Hydrolyze Arabinosyl from Either Mono-or Disubstituted Xylosyl Units in Wheat Arabinoxylan.International journal of molecular sciences · 2022Article
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- Characterisation of three novel α-L-arabinofuranosidases from a compost metagenome.BMC biotechnology · 2019Article
- The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans.Biotechnology for biofuels · 2018Article
- Identification of the nucleophile catalytic residue of GH51 α-L-arabinofuranosidase from Pleurotus ostreatus.AMB Express · 2015Article
- Characterization of a hexameric exo-acting GH51 α-l-arabinofuranosidase from the mesophilic Bacillus subtilis.Molecular biotechnology · 2013Article
- Two structurally discrete GH7-cellobiohydrolases compete for the same cellulosic substrate fiber.Biotechnology for biofuels · 2012Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-L-arabinofuranosidases (EC 3.2.1.55) participate in the degradation of a variety of L-arabinose-containing polysaccharides and interact synergistically with other hemicellulases in the production of oligosaccharides and bioconversion of lignocellulosic biomass into biofuels. In this work, the structure of a novel thermostable family 51 (GH51) α-L-arabinofuranosidase from Thermotoga petrophila RKU-1 (TpAraF) was determined at 3.1 Å resolution. The TpAraF tertiary structure consists of an (α/β)-barrel catalytic core associated with a C-terminal β-sandwich domain, which is stabilized by hydrophobic contacts. In contrast to other structurally characterized GH51 AraFs, the accessory domain of TpAraF is intimately linked to the active site by a long β-hairpin motif, which modifies the catalytic cavity in shape and volume. Sequence and structural analyses indicate that this motif is unique to Thermotoga AraFs. Small angle X-ray scattering investigation showed that TpAraF assembles as a hexamer in solution and is preserved at the optimum catalytic temperature, 65°C, suggesting functional significance. Crystal packing analysis shows that the biological hexamer encompasses a dimer of trimers and the multiple oligomeric interfaces are predominantly fashioned by polar and electrostatic contacts.
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