5WD9
Crystal structure of Legionella pneumophila effector lpg2328
Summary for 5WD9
| Entry DOI | 10.2210/pdb5wd9/pdb |
| Descriptor | Lem22 (2 entities in total) |
| Functional Keywords | bacterial effector, legionella, protein binding, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi |
| Biological source | Legionella pneumophila subsp. pneumophila ATCC 43290 |
| Total number of polymer chains | 1 |
| Total formula weight | 10529.94 |
| Authors | Kozlov, G.,Wong, K.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2017-07-04, release date: 2017-11-29, Last modification date: 2024-04-03) |
| Primary citation | Kozlov, G.,Wong, K.,Gehring, K. Crystal structure of the Legionella effector Lem22. Proteins, 86:263-267, 2018 Cited by PubMed Abstract: Legionella pneumophila is a pathogen causing severe pneumonia in humans called Legionnaires' disease. Lem22 is a previously uncharacterized effector protein conserved in multiple Legionella strains. Here, we report the crystal structure of Lem22 from the Philadelphia strain, also known as lpg2328, at 1.40 Å resolution. The structure shows an up-and-down three-helical bundle with a significant structural similarity to a number of protein-binding domains involved in apoptosis and membrane trafficking. Sequence conservation identifies a putative functional site on the interface of helices 2 and 3. The structure is an important step toward a functional characterization of Lem22. PubMed: 29159828DOI: 10.1002/prot.25427 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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