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Black, Miles H; Osinski, Adam; Gradowski, Marcin; Servage, Kelly A; Pawłowski, Krzysztof; Tomchick, Diana R; Tagliabracci, Vincent S
Science, 05/2019, Volume: 364, Issue: 6442Journal Article
Enzymes with a protein kinase fold transfer phosphate from adenosine 5'-triphosphate (ATP) to substrates in a process known as phosphorylation. Here, we show that the meta-effector SidJ adopts a protein kinase fold, yet unexpectedly catalyzes protein polyglutamylation. SidJ is activated by host-cell calmodulin to polyglutamylate the SidE family of ubiquitin (Ub) ligases. Crystal structures of the SidJ-calmodulin complex reveal a protein kinase fold that catalyzes ATP-dependent isopeptide bond formation between the amino group of free glutamate and the γ-carboxyl group of an active-site glutamate in SidE. We show that SidJ polyglutamylation of SidE, and the consequent inactivation of Ub ligase activity, is required for successful replication in a viable eukaryotic host cell.
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