Structural highlights
Publication Abstract from PubMed
Persistence and replication of the gram-negative bacterium Legionella pneumophila in the human host cell depend on so-called effector proteins that target diverse cellular functions and modulate them in favor of the pathogen. We solved the crystal structure of the L. pneumophila effector protein MesI de novo to a resolution of 2.2 A. The 34 kDa polypeptide chain folds into two distinct alpha-helical domains. The larger C-terminal domain shows similarity to tetratricopeptide repeat proteins. Using size-exclusion chromatography, we confirmed that MesI binds tightly to full-length SidI and that deletion of either the N- or the C-terminus weakens the interaction. Based on the three-dimensional structure of MesI we suggest a possible binding mode for SidI and identified two homologs of MesI within the proteome of L. pneumophila that do not bind to SidI, but may act as specific inhibitors of other yet to be identified effectors.
Crystal structure of the metaeffector MesI (Lpg2505) from Legionella pneumophila.,Machtens DA, Willerding JM, Eschenburg S, Reubold TF Biochem Biophys Res Commun. 2020 Jun 30;527(3):696-701. doi:, 10.1016/j.bbrc.2020.05.027. Epub 2020 May 15. PMID:32423822[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Machtens DA, Willerding JM, Eschenburg S, Reubold TF. Crystal structure of the metaeffector MesI (Lpg2505) from Legionella pneumophila. Biochem Biophys Res Commun. 2020 Jun 30;527(3):696-701. doi:, 10.1016/j.bbrc.2020.05.027. Epub 2020 May 15. PMID:32423822 doi:http://dx.doi.org/10.1016/j.bbrc.2020.05.027
