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<p>The two effectors LnaB and MavL of <i>Legionella pneumophila</i> coordinate the conversion of phosphoribosyl ubiquitin (PR-Ub) released by reversal of ubiquitination induced by members of the SidE effector family into functional Ub. LnaB acts as an actin-dependent phosphoryl AMPylase that converts PR-Ub into ADP-ribosylated (ADPR)-Ub. Catalysis by LnaB requires the conserved SHE motif present in a large family of bacterial toxins. Here we describe a series of structures of LnaB in complex with the cofactor actin and the substrate PR-Ub and ATP. LnaB harbors both adenylyltransferase and ATPase activities, which reveal an adenylylation mechanism involved in a two-step catalytic process. Actin performs a unique activation mechanism that promotes the recruitment of PR-Ub by LnaB to activate LnaB’s ATPase activity through interacting with LnaB and PR-Ub. Mechanisms derived from this series of structures covering the process of LnaB action establish an important biochemical basis for protein AMPylation.</p><p></p>

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Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase

  • 期刊论文

  • 发表日期：

    2025年6月30日

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  • Tao-Tao Chen,
  • Qiuhua Lu,
  • Si-Ru Zheng,
  • Jiaqi Fu,
  • Jing Chen,
  • Lina Kang,
  • Juhong Wu,
  • Jiwei Luo,
  • Jiangyang Tong,
  • Siying Li,
  • Xiangliang Li,
  • Shan Li,
  • Jinyu Li,
  • Shaoyuan Wang,
  • Yue Feng,
  • Zhao-Qing Luo,
  • Songying Ouyang

摘要

The two effectors LnaB and MavL of Legionella pneumophila coordinate the conversion of phosphoribosyl ubiquitin (PR-Ub) released by reversal of ubiquitination induced by members of the SidE effector family into functional Ub. LnaB acts as an actin-dependent phosphoryl AMPylase that converts PR-Ub into ADP-ribosylated (ADPR)-Ub. Catalysis by LnaB requires the conserved SHE motif present in a large family of bacterial toxins. Here we describe a series of structures of LnaB in complex with the cofactor actin and the substrate PR-Ub and ATP. LnaB harbors both adenylyltransferase and ATPase activities, which reveal an adenylylation mechanism involved in a two-step catalytic process. Actin performs a unique activation mechanism that promotes the recruitment of PR-Ub by LnaB to activate LnaB’s ATPase activity through interacting with LnaB and PR-Ub. Mechanisms derived from this series of structures covering the process of LnaB action establish an important biochemical basis for protein AMPylation.