7YJI
Crystal structure of Lpg1083 from Legionella pneumophila
Summary for 7YJI
Entry DOI | 10.2210/pdb7yji/pdb |
Descriptor | T4SS effector Lpg1083, ACETATE ION (3 entities in total) |
Functional Keywords | t4ss effector, nuclear-localization, lamin-b2, importin-13, apoptosis |
Biological source | Legionella pneumophila |
Total number of polymer chains | 1 |
Total formula weight | 27602.54 |
Authors | |
Primary citation | 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 Cited by 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: 37253620DOI: 10.1093/jmcb/mjad036 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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