| Literature DB >> 29159828 |
Guennadi Kozlov1, Kathy Wong1, Kalle Gehring1.
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.Entities:
Keywords: Legionella; X-ray crystallography; lpg2328; pathogen; virulence factor
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Year: 2017 PMID: 29159828 PMCID: PMC5897132 DOI: 10.1002/prot.25427
Source DB: PubMed Journal: Proteins ISSN: 0887-3585