6OQQ
Legionella pneumophila SidJ/Saccharomyces cerevisiae calmodulin complex
Summary for 6OQQ
| Entry DOI | 10.2210/pdb6oqq/pdb |
| Descriptor | Legionella pneumophila SidJ, Calmodulin, ADENOSINE MONOPHOSPHATE, ... (9 entities in total) |
| Functional Keywords | polyglutamylation, pseudokinase, atypical kinase fold, transferase |
| Biological source | Legionella pneumophila More |
| Total number of polymer chains | 4 |
| Total formula weight | 235378.17 |
| Authors | Tomchick, D.R.,Tagliabracci, V.S.,Black, M.,Osinski, A. (deposition date: 2019-04-28, release date: 2019-05-15, Last modification date: 2024-03-13) |
| Primary citation | Black, M.H.,Osinski, A.,Gradowski, M.,Servage, K.A.,Pawlowski, K.,Tomchick, D.R.,Tagliabracci, V.S. Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases. Science, 364:787-792, 2019 Cited by PubMed Abstract: 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. PubMed: 31123136DOI: 10.1126/science.aaw7446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.102 Å) |
Structure validation
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