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 () and Zhi-Min Zhang ()
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Yao Xia: Jinan University
Rongfeng Zou: Chinese Academy of Sciences
Maxime Escouboué: Université de Toulouse
Liang Zhong: Jinan University
Chengjun Zhu: Jinan University
Cécile Pouzet: Université de Toulouse, CNRS
Xueqiang Wu: Jinan University
Yongjin Wang: Jinan University
Guohua Lv: Jinan University
Haibo Zhou: Jinan University
Pinghua Sun: Jinan University
Ke Ding: Jinan University
Laurent Deslandes: Université de Toulouse
Shuguang Yuan: Chinese Academy of Sciences
Zhi-Min Zhang: Jinan University

Nature Communications, 2021, vol. 12, issue 1, 1-10

Abstract: Abstract 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. Structural comparison of apo-PopP2 with the InsP6-bound PopP2 reveals a substantial conformational readjustment centered in the substrate-binding site. Combining biochemical and computational analyses, we further identify a mechanism by which the association of InsP6 with PopP2 induces 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. Together, our study uncovers the molecular basis governing InsP6-mediated allosteric regulation of YopJ family acetyltransferases and further expands the paradigm of fold-switching proteins.

Date: 2021
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DOI: 10.1038/s41467-021-26183-1

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