Fujimoto Zui, Ichinose Hitomi, Harazono Koichi, Honda Mariko, Uzura Atsuko, Kaneko Satoshi
Protein Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):632-4. doi: 10.1107/S1744309109017230. Epub 2009 May 23.
Beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893 is a monomeric protein consisting of a catalytic domain belonging to glycosyl hydrolase family 27, an unknown domain and a substrate-binding domain belonging to carbohydrate-binding module family 13. The complete enzyme (residues 45-658) has successfully been cloned and homologously expressed in the Streptomyces expression system. beta-L-Arabinopyranosidase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 1.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.2, b = 98.9, c = 181.3 A. The Matthews coefficient was calculated to be 2.38 A(3) Da(-1).
来自阿维链霉菌NBRC14893的β-L-阿拉伯吡喃糖苷酶是一种单体蛋白,由属于糖基水解酶家族27的催化结构域、一个未知结构域和属于碳水化合物结合模块家族13的底物结合结构域组成。完整的酶(45-658位氨基酸残基)已成功克隆并在链霉菌表达系统中进行同源表达。β-L-阿拉伯吡喃糖苷酶通过坐滴气相扩散法结晶。晶体衍射分辨率达到1.6 Å,属于空间群P2(1)2(1)2(1),晶胞参数a = 68.2,b = 98.9,c = 181.3 Å。马修斯系数计算为2.38 Å(3) Da(-1)。