7YJI

Crystal structure of Lpg1083 from Legionella pneumophila

7YJI の概要

• エントリーDOI: 10.2210/pdb7yji/pdb
• 分子名称: T4SS effector Lpg1083, ACETATE ION (3 entities in total)
• 機能のキーワード: t4ss effector, nuclear-localization, lamin-b2, importin-13, apoptosis
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27602.54

構造登録者

Ge, H.,Gao, J.,Chen, X. (登録日: 2022-07-20, 公開日: 2023-06-28, 最終更新日: 2023-12-27)

主引用文献

Gao, J.,Xu, W.,Tang, F.,Xu, M.,Zhou, Q.,Yang, X.,Zhang, N.,Ma, J.,Yang, Q.,Chen, X.,Qin, X.,Ge, H.
The bacterial effector SidN/Lpg1083 promotes cell death by targeting Lamin-B2.
J Mol Cell Biol, 15:-, 2023

PubMed Abstract: To facilitate survival, replication, and dissemination, the intracellular pathogen Legionella pneumophila relies on its unique type IVB secretion system (T4SS) to deliver over 330 effectors to hijack host cell pathways in a spatiotemporal manner. The effectors and their host targets are largely unexplored due to their low sequence identity to the known proteins and functional redundancy. The T4SS effector SidN (Lpg1083) is secreted into host cells during the late infection period. However, to the best of our knowledge, the molecular characterization of SidN has not been studied. Herein, we identified SidN as a nuclear envelope-localized effector. Its structure adopts a novel fold, and the N-terminal domain is crucial for its specific subcellular localization. Furthermore, we found that SidN is transported by eukaryotic karyopherin Importin-13 into the nucleus, where it attaches to the N-terminal region of Lamin-B2 to interfere with the integrity of the nuclear envelope, causing nuclear membrane disruption and eventually cell death. Our work provides new insights into the structure and function of an L. pneumophila effector protein, and suggests a potential strategy utilized by the pathogen to promote host cell death and then escape from the host for secondary infection.

PubMed: 37253620
DOI: 10.1093/jmcb/mjad036

実験手法

X-RAY DIFFRACTION (2.1 Å)