6K4R
Crystal structure of SidJ-CaM-AMP ternary complex at 3.11 A
Summary for 6K4R
| Entry DOI | 10.2210/pdb6k4r/pdb |
| Descriptor | SidJ, Calmodulin-1, ADENOSINE MONOPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | a novel kinase, transferase, transferase-cell cycle complex, transferase/cell cycle |
| Biological source | Legionella pneumophila subsp. pneumophila str. Philadelphia 1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 235686.89 |
| Authors | Ouyang, S.Y. (deposition date: 2019-05-26, release date: 2019-07-24, Last modification date: 2024-03-27) |
| Primary citation | Gan, N.,Zhen, X.,Liu, Y.,Xu, X.,He, C.,Qiu, J.,Liu, Y.,Fujimoto, G.M.,Nakayasu, E.S.,Zhou, B.,Zhao, L.,Puvar, K.,Das, C.,Ouyang, S.,Luo, Z.Q. Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase. Nature, 572:387-391, 2019 Cited by PubMed Abstract: The bacterial pathogen Legionella pneumophila creates an intracellular niche permissive for its replication by extensively modulating host-cell functions using hundreds of effector proteins delivered by its Dot/Icm secretion system. Among these, members of the SidE family (SidEs) regulate several cellular processes through a unique phosphoribosyl ubiquitination mechanism that bypasses the canonical ubiquitination machinery. The activity of SidEs is regulated by another Dot/Icm effector known as SidJ; however, the mechanism of this regulation is not completely understood. Here we demonstrate that SidJ inhibits the activity of SidEs by inducing the covalent attachment of glutamate moieties to SdeA-a member of the SidE family-at E860, one of the catalytic residues that is required for the mono-ADP-ribosyltransferase activity involved in ubiquitin activation. This inhibition by SidJ is spatially restricted in host cells because its activity requires the eukaryote-specific protein calmodulin (CaM). We solved a structure of SidJ-CaM in complex with AMP and found that the ATP used in this reaction is cleaved at the α-phosphate position by SidJ, which-in the absence of glutamate or modifiable SdeA-undergoes self-AMPylation. Our results reveal a mechanism of regulation in bacterial pathogenicity in which a glutamylation reaction that inhibits the activity of virulence factors is activated by host-factor-dependent acyl-adenylation. PubMed: 31330531DOI: 10.1038/s41586-019-1439-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.109 Å) |
Structure validation
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