Tatiana A.C.B. Souza and Camila R. Santos contributed equally to this work.
Protein Structure Report
Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1†
Article first published online: 3 AUG 2011
Copyright © 2011 The Protein Society
Volume 20, Issue 9, pages 1632–1637, September 2011
How to Cite
Souza, T. A.C.B., Santos, C. R., Souza, A. R., Oldiges, D. P., Ruller, R., Prade, R. A., Squina, F. M. and Murakami, M. T. (2011), Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1. Protein Science, 20: 1632–1637. doi: 10.1002/pro.693
RAP and FMS are authors of patent WO 2010/083518 A2 licensed to Edenspace Corporation, US.
- Issue published online: 17 AUG 2011
- Article first published online: 3 AUG 2011
- Accepted manuscript online: 27 JUL 2011 10:29AM EST
- Manuscript Accepted: 1 JUL 2011
- Manuscript Received: 19 MAY 2011
- Fundação de Amparo a Pesquisa do Estado de São Paulo
- Conselho Nacional de Desenvolvimento Científico e Tecnológico
- US Department of Energy
- glycosyl hydrolase family 51;
- thermostable α-L-arabinofuranosidase;
- Thermotoga petrophila RKU-1
α-L-arabinofuranosidases (EC 18.104.22.168) 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.