Miyanaga Akimasa, Koseki Takuya, Matsuzawa Hiroshi, Wakagi Takayoshi, Shoun Hirofumi, Fushinobu Shinya
Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1286-8. doi: 10.1107/S0907444904010108. Epub 2004 Jun 22.
Alpha-L-Arabinofuranosidase (EC 3.2.1.55) is one of the hemicellulases that cleave the glycosidic bonds between L-arabinofuranoside side chains and various oligosaccharides. In this study, the first crystallization and preliminary X-ray analysis of alpha-L-arabinofuranosidase B from Aspergillus kawachii IFO4308 (AkAbfB), a family 54 glycoside hydrolase, is described. Recombinant AkAbfB was expressed in Escherichia coli and Pichia pastoris. The native crystals of recombinant AkAbfB produced by P. pastoris belong to the orthorhombic space group P2(1)2(1)2(1) (unit-cell parameters a = 39.5, b = 98.2, c = 144.0 A) and diffracted X-rays to a resolution of 1.82 A.
α-L-阿拉伯呋喃糖苷酶（EC 3.2.1.55）是一种半纤维素酶，可裂解L-阿拉伯呋喃糖苷侧链与各种寡糖之间的糖苷键。在本研究中，描述了来自河合曲霉IFO4308（AkAbfB）的α-L-阿拉伯呋喃糖苷酶B（一种54家族糖苷水解酶）的首次结晶和初步X射线分析。重组AkAbfB在大肠杆菌和毕赤酵母中表达。毕赤酵母产生的重组AkAbfB的天然晶体属于正交晶系空间群P2(1)2(1)2(1)（晶胞参数a = 39.5，b = 98.2，c = 144.0 Å），X射线衍射分辨率为1.82 Å。
