Liu Wenting, Sun Yu, Ko Tzu-Ping, Wiegel Juergen, Shao Weilan, Lu Fuping, Guo Rey-Ting, Huang Chun-Hsiang
Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Aug 1;68(Pt 8):914-6. doi: 10.1107/S1744309112025328. Epub 2012 Jul 31.
Xylosidases hydrolyze xylopolymers at the nonreducing end to free xylose units. The β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485 was expressed in Escherichia coli and the recombinant protein was purified and crystallized. A BLASTP search with the XylC protein sequence showed that no similar structure had previously been solved. XylC was classified as a member of the new glycoside hydrolase family GH120 according to the CAZy website (http://www.cazy.org/). Crystals belonging to the monoclinic space group P2(1), with unit-cell parameters a = 88.36, b = 202.20, c = 99.87 Å, β = 99.04°, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 Å resolution. Structure determination using MIR and MAD methods is in progress.
木糖苷酶在非还原端水解木聚糖聚合物，释放出木糖单元。嗜糖热厌氧杆菌JW/SL-YS485的β-木糖苷酶（XylC）在大肠杆菌中表达，重组蛋白经纯化和结晶。对XylC蛋白序列进行BLASTP搜索表明，此前尚未解析出类似结构。根据CAZy网站（http://www.cazy.org/），XylC被归类为新的糖苷水解酶家族GH120的成员。通过坐滴气相扩散法获得了属于单斜空间群P2(1)的晶体，其晶胞参数为a = 88.36、b = 202.20、c = 99.87 Å、β = 99.04°，衍射分辨率达到2.2 Å。目前正在使用MIR和MAD方法进行结构测定。
