Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA

Xiaoyun Yang, Zongqiang Li, Liang Zhao, Zhun She, Zengqiang Gao, Sen-Fang Sui (), Yuhui Dong () and Yanhua Li ()
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Xiaoyun Yang: Southern University of Science and Technology
Zongqiang Li: Southern University of Science and Technology
Liang Zhao: Southern University of Science and Technology
Zhun She: Chinese Academy of Sciences
Zengqiang Gao: Chinese Academy of Sciences
Sen-Fang Sui: Southern University of Science and Technology
Yuhui Dong: Chinese Academy of Sciences
Yanhua Li: Chinese Academy of Sciences

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract PldA, a phospholipase D (PLD) effector, catalyzes hydrolysis of the phosphodiester bonds of glycerophospholipids—the main component of cell membranes—and assists the invasion of the opportunistic pathogen Pseudomonas aeruginosa. As a cognate immunity protein, PA3488 can inhibit the activity of PldA to avoid self-toxicity. However, the precise inhibitory mechanism remains elusive. We determine the crystal structures of full-length and truncated PldA and the cryogenic electron microscopy structure of the PldA–PA3488 complex. Structural analysis reveals that there are different intermediates of PldA between the “open” and “closed” states of the catalytic pocket, accompanied by significant conformational changes in the “lid” region and the peripheral helical domain. Through structure-based mutational analysis, we identify the key residues responsible for the enzymatic activity of PldA. Together, these data provide an insight into the molecular mechanisms of PldA invasion and its neutralization by PA3488, aiding future design of PLD-targeted inhibitors and drugs.

Date: 2022
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DOI: 10.1038/s41467-022-33690-2

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