6PLM

Legionella pneumophila SidJ/ Calmodulin 2 complex

6PLM の概要

• エントリーDOI: 10.2210/pdb6plm/pdb
• 分子名称: SidJ protein, Calmodulin-2, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: sidj, calmodulin, polyglutamylation, pseudokinase, transferase
• 由来する生物種: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 209273.31

構造登録者

Mao, Y.,Sulpizio, A.,Minelli, M.E.,Wu, X. (登録日: 2019-07-01, 公開日: 2019-11-20, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.592 Å)