Crystal structure of the <i>Legionella pneumophila</i> effector SidL (Lpg0437) in complex with its metaeffector LegA11 (Lpg0436).

ABSTRACT: Legionella pneumophila is an opportunistic human pathogen that causes atypical pneumonia called Legionnaires' Disease. To replicate within host cells, L. pneumophila injects up to 330 effector proteins into the host cytosol via a Dot/Icm type IV secretion system. Several effectors, called metaeffectors, regulate the activity of other effectors within infected host cells through direct protein-protein interactions. LegA11 (AnkJ/Lpg0436) has been identified as a putative metaeffector of SidL (Ceg14/Lpg0437), one of eight L. pneumophila effectors that inhibit host mRNA translation. LegA11 binds and suppresses SidL enzymatic activity, but the molecular basis of this regulation and impact on mRNA translation are unknown. Here, we present the crystal structure of SidL in com

SUBMITTER: Machtens DA 

PROVIDER: S-EPMC12633379 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature