Structural highlights
Publication Abstract from PubMed
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 A 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.
Crystal structure of the Legionella effector Lem22.,Kozlov G, Wong K, Gehring K Proteins. 2017 Nov 21. doi: 10.1002/prot.25427. PMID:29159828[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kozlov G, Wong K, Gehring K. Crystal structure of the Legionella effector Lem22. Proteins. 2017 Nov 21. doi: 10.1002/prot.25427. PMID:29159828 doi:http://dx.doi.org/10.1002/prot.25427