6YVG
Crystal structure of MesI (Lpg2505) from Legionella pneumophila
Summary for 6YVG
| Entry DOI | 10.2210/pdb6yvg/pdb |
| Descriptor | MesI (Lpg2505), 1,2-ETHANEDIOL, IODIDE ION, ... (4 entities in total) |
| Functional Keywords | protein binding |
| Biological source | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Total number of polymer chains | 1 |
| Total formula weight | 35352.45 |
| Authors | Machtens, D.A.,Willerding, J.M.,Eschenburg, S.,Reubold, T.F. (deposition date: 2020-04-28, release date: 2020-06-10, Last modification date: 2024-05-15) |
| Primary citation | Machtens, D.A.,Willerding, J.M.,Eschenburg, S.,Reubold, T.F. Crystal structure of the metaeffector MesI (Lpg2505) from Legionella pneumophila. Biochem.Biophys.Res.Commun., 527:696-701, 2020 Cited by PubMed Abstract: 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 Å. The 34 kDa polypeptide chain folds into two distinct α-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. PubMed: 32423822DOI: 10.1016/j.bbrc.2020.05.027 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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