Yao Xia, Rongfeng Zou, Maxime Escouboué, Liang Zhong, Chengjun Zhu, Cécile Pouzet, Xueqiang Wu, Yongjin Wang, Guohua Lv, Haibo Zhou, Pinghua Sun, Ke Ding, Laurent Deslandes, Shuguang Yuan, Zhi-Min Zhang
The Yersinia outer protein J (YopJ) family effectors are widely deployed through the type III secretion system by both plant and animal pathogens. As non-canonical acetyltransferases, the enzymatic activities of YopJ family effectors are allosterically activated by the eukaryote-specific ligand inositol hexaphosphate (InsP6). However, the underpinning molecular mechanism remains undefined. Here we present the crystal structure of apo-PopP2, a YopJ family member secreted by the plant pathogen Ralstonia solanacearum...
October 13, 2021: Nature Communications