Crystal structure of the Legionella effector Lem22.
Guennadi KozlovKathy WongKalle GehringPublished in: Proteins (2017)
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.
Keyphrases
- amino acid
- regulatory t cells
- binding protein
- acute lymphoblastic leukemia
- dendritic cells
- protein protein
- oxidative stress
- escherichia coli
- endoplasmic reticulum stress
- transcription factor
- type iii
- early onset
- intensive care unit
- single molecule
- candida albicans
- immune response
- cell proliferation
- dna binding
- signaling pathway
- pi k akt