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

摘要

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 (). 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 () of the Protein Data Bank did not reveal any similar crystal structures. Structural determination by using SeMet MAD and MIR methods is in progress.