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

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.
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Contributor : Laurent Deslandes Connect in order to contact the contributor
Submitted on : Wednesday, August 10, 2022 - 12:43:43 PM
Last modification on : Thursday, August 11, 2022 - 3:50:57 AM

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Yao Xia, Rongfeng Zou, Maxime Escouboué, Liang Zhong, Chengjun Zhu, et al.. Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase. Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.5969. ⟨10.1038/s41467-021-26183-1⟩. ⟨hal-03749090⟩



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