7V53

Crystal structure of full-length phospholipase D from Pseudomonas aeruginosa PAO1

7V53 の概要

• エントリーDOI: 10.2210/pdb7v53/pdb
• 分子名称: Phospholipase D (2 entities in total)
• 機能のキーワード: phospholipase d, toxin, hydrolase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 122478.06

構造登録者

Yang, Y.,Li, Z. (登録日: 2021-08-16, 公開日: 2022-08-17, 最終更新日: 2024-11-06)

主引用文献

Yang, X.,Li, Z.,Zhao, L.,She, Z.,Gao, Z.,Sui, S.F.,Dong, Y.,Li, Y.
Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA.
Nat Commun, 13:5979-5979, 2022

PubMed 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.

PubMed: 36216841
DOI: 10.1038/s41467-022-33690-2

実験手法

X-RAY DIFFRACTION (2.1 Å)