Crystallization and preliminary X-ray diffraction analysis of a novel β-l-arabinofuranosidase (HypBA1) from Bifidobacterium longum

The β-l-arabinofuranosidase (HypBA1) from Bifidobacterium longum JCM 1217 hydrolyzes the β-1,2-linked arabinofuranose disaccharide to release l-arabinoses. HypBA1 was classified into glycoside hydrolase family 127 (GH127) by the CAZy website (http://www.cazy.org/). The enzyme was expressed in Escherichia coli and the purified recombinant protein was crystallized. Crystals belonging to the primitive hexagonal space group P3x21, with unit-cell parameters a = b = 75.9, c = 254.0 Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.78 Å resolution. A BLASTP search (http://blast.ncbi.nlm.nih.gov/) of the Protein Data Bank did not reveal any similar crystal structures. Structural determination by using SeMet MAD and MIR methods is in progress.

Source: Acta Crystallographica Section F - April 17, 2014 Category: Biochemistry Authors: Zhu, Z.He, M.Huang, C.-H.Ko, T.-P.Zeng, Y.-F.Huang, Y.-N.Jia, S.Lu, F.Liu, J.-R.Guo, R.-T. Tags: hydroxyproline-rich glycoproteins glycoside hydrolase HypBA1 Bifidobacterium longum crystallization communications Source Type: research