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Crystal structure of the Legionella effector Lem22.

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.

SUBMITTER: Kozlov G

PROVIDER: S-EPMC5897132 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Crystal structure of the Legionella effector Lem22.

Kozlov Guennadi G Wong Kathy K Gehring Kalle K

Proteins 20171129 2

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 traffick ...[more]

PMID: 29159828

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