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Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase


Our recent work which is entitled "Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase" has been published in Nature Communications. In this work, it is the first time that we found a new mechanism for Yersinia outer protein J (YopJ) family effectors of bacteria to execute their physiological functions.

In this study, InsP6 with PopP2 were demonstrated to induce an α-helix-to-β-strand transition in the catalytic core, resulting in stabilization of the substrate recognition helix in the target protein binding site. Such mechanism could help bacteria to escape the host immune system recognizing outside invade. This might finally result in drug resistance as well.

Our new findings provide a new insight to the next generation antibiotics new drug discovery.

Related work
Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase. 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* , Nature Communications (2021) doi: 10.1038/s41467-021-26183-1

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