Author response: Protein polyglutamylation catalyzed by the bacterial calmodulin-dependent pseudokinase SidJ

The kinase domain transfers phosphate from ATP to substrates. However, the Legionella effector SidJ adopts a kinase fold yet catalyzes calmodulin (CaM)-dependent glutamylation to inactivate the SidE ubiquitin ligases. The structural and mechanistic basis in which the kinase domain catalyzes protein glutamylation is unknown. Here we present cryo-EM reconstructions of SidJ:CaM:SidE reaction intermediate complexes. We show that the kinase-like active site of SidJ adenylates an active site Glu in SidE resulting in the formation of a stable reaction intermediate complex. An insertion in the catalytic loop of the kinase domain positions the donor Glu near the acyl-adenylate for peptide bond formation. Our structural analysis led us to discover that the SidJ paralog SdjA is a glutamylase that differentially regulates the SidE-ligases during Legionella infection. Our results uncover the structural and mechanistic basis in which the kinase fold catalyzes non-ribosomal amino acid ligations and reveal an unappreciated level of SidE-family regulation.

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Author response: Protein polyglutamylation catalyzed by the bacterial calmodulin-dependent pseudokinase SidJ

Cited by 2 publications

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There’s more to death than life: Noncatalytic functions in kinase and pseudokinase signaling

There’s more to death than life: Noncatalytic functions in kinase and pseudokinase signaling

Structural and mechanistic basis for protein glutamylation by the kinase fold

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