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Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1.

Authors
  • Souza, Tatiana A C B
  • Santos, Camila R
  • Souza, Angelica R
  • Oldiges, Daiane P
  • Ruller, Roberto
  • Prade, Rolf A
  • Squina, Fabio M
  • Murakami, Mario T
Type
Published Article
Journal
Protein Science
Publisher
Wiley (John Wiley & Sons)
Publication Date
Sep 01, 2011
Volume
20
Issue
9
Pages
1632–1637
Identifiers
DOI: 10.1002/pro.693
PMID: 21796714
Source
Medline
License
Unknown

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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