Delsaute Maud, Berlemont Renaud, Dehareng Dominique, Van Elder Dany, Galleni Moreno, Bauvois Cédric
Centre d'Ingénierie des Protéines, Laboratoire de Macromolécules Biologiques, Université de Liège (ULg), Bâtiment B6, Allée de la Chimie 3, 4000 Liège, Belgium.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):828-33. doi: 10.1107/S1744309113014565. Epub 2013 Jul 26.
RBcel1 is an endoglucanase belonging to glycoside hydrolase family 5 subfamily 5 (GH5_5) that was recently identified from a soil metagenome library from the Antarctic. Unlike its closest structural homologue (Cel5A from Thermoascus aurantiacus), this enzyme was reported to be able to catalyze transglycosylation reactions and has putatively been implicated in the bacterial cellulose-synthesis process. Here, the structure of RBcel1 at 1.4 Å resolution, solved by molecular replacement, is reported. The structure and putative substrate-binding site are described and compared with those of other GH5_5 subfamily members.
RBcel1是一种属于糖苷水解酶家族5亚家族5（GH5_5）的内切葡聚糖酶，最近从南极土壤宏基因组文库中鉴定出来。与其最接近的结构同源物（来自橙色嗜热子囊菌的Cel5A）不同，据报道这种酶能够催化转糖基化反应，并且可能参与细菌纤维素合成过程。本文报道了通过分子置换法解析的分辨率为1.4 Å的RBcel1结构。描述了该结构和假定的底物结合位点，并与其他GH5_5亚家族成员的结构进行了比较。
