6OQQ

Legionella pneumophila SidJ/Saccharomyces cerevisiae calmodulin complex

6OQQ の概要

• エントリーDOI: 10.2210/pdb6oqq/pdb
• 分子名称: Legionella pneumophila SidJ, Calmodulin, ADENOSINE MONOPHOSPHATE, ... (9 entities in total)
• 機能のキーワード: polyglutamylation, pseudokinase, atypical kinase fold, transferase
• 由来する生物種: Legionella pneumophila; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 235378.17

構造登録者

Tomchick, D.R.,Tagliabracci, V.S.,Black, M.,Osinski, A. (登録日: 2019-04-28, 公開日: 2019-05-15, 最終更新日: 2024-03-13)

主引用文献

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

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: 31123136
DOI: 10.1126/science.aaw7446

実験手法

X-RAY DIFFRACTION (2.102 Å)