3S2C

Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1

Summary for 3S2C

• Entry DOI: 10.2210/pdb3s2c/pdb
• Descriptor: Alpha-N-arabinofuranosidase (2 entities in total)
• Functional Keywords: tim-barrel and jelly-roll domains, alpha-l-arabinofuranosidase, glycosyl hydrolase 51 family, hydrolase
• Biological source: Thermotoga petrophila
• Total number of polymer chains: 12
• Total formula weight: 664184.48

Authors

Souza, T.A.C.B.,Santos, C.R.,Souza, A.R.,Oldiges, D.P.,Ruller, R.,Prade, R.A.,Squina, F.M.,Murakami, M.T. (deposition date: 2011-05-16, release date: 2012-02-01, Last modification date: 2023-09-13)

Primary citation

Souza, T.A.,Santos, C.R.,Souza, A.R.,Oldiges, D.P.,Ruller, R.,Prade, R.A.,Squina, F.M.,Murakami, M.T.
Structure of a novel thermostable GH51 Alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1
Protein Sci., 20:1632-1637, 2011

PubMed 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.

PubMed: 21796714
DOI: 10.1002/pro.693

Experimental method

X-RAY DIFFRACTION (3 Å)