6PLM

Legionella pneumophila SidJ/ Calmodulin 2 complex

Summary for 6PLM

• Entry DOI: 10.2210/pdb6plm/pdb
• Descriptor: SidJ protein, Calmodulin-2, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: sidj, calmodulin, polyglutamylation, pseudokinase, transferase
• Biological source: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513); More
• Total number of polymer chains: 4
• Total formula weight: 209273.31

Authors

Mao, Y.,Sulpizio, A.,Minelli, M.E.,Wu, X. (deposition date: 2019-07-01, release date: 2019-11-20, Last modification date: 2024-03-13)

Primary citation

Sulpizio, A.,Minelli, M.E.,Wan, M.,Burrowes, P.D.,Wu, X.,Sanford, E.J.,Shin, J.H.,Williams, B.C.,Goldberg, M.L.,Smolka, M.B.,Mao, Y.
Protein polyglutamylation catalyzed by the bacterial calmodulin-dependent pseudokinase SidJ.
Elife, 8:-, 2019

PubMed Abstract: Pseudokinases are considered to be the inactive counterparts of conventional protein kinases and comprise approximately 10% of the human and mouse kinomes. Here, we report the crystal structure of the effector protein, SidJ, in complex with the eukaryotic Ca-binding regulator, calmodulin (CaM). The structure reveals that SidJ contains a protein kinase-like fold domain, which retains a majority of the characteristic kinase catalytic motifs. However, SidJ fails to demonstrate kinase activity. Instead, mass spectrometry and in vitro biochemical analyses demonstrate that SidJ modifies another effector SdeA, an unconventional phosphoribosyl ubiquitin ligase, by adding glutamate molecules to a specific residue of SdeA in a CaM-dependent manner. Furthermore, we show that SidJ-mediated polyglutamylation suppresses the ADP-ribosylation activity. Our work further implies that some pseudokinases may possess ATP-dependent activities other than conventional phosphorylation.

PubMed: 31682223
DOI: 10.7554/eLife.51162

Experimental method

X-RAY DIFFRACTION (2.592 Å)