Crystal structure of the Legionella effector Lem22 |
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| Authors: | Kalle Gehring |
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| Affiliation: | Department of Biochemistry, Groupe de recherche axé sur la structure des protéines, McGill University, Montreal, QC, Canada |
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| 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. |
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| Keywords: | Legionella lpg2328 pathogen virulence factor X‐ray crystallography |
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