Crystal structure of the Legionella pneumophila Lem10 effector reveals a new member of the HD protein superfamily.

ABSTRACT: Legionella pneumophila, the intracellular pathogen that can cause severe pneumonia known as Legionnaire's disease, translocates close to 300 effectors inside the host cell using Dot/Icm type IVB secretion system. The structure and function for the majority of these effector proteins remains unknown. Here, we present the crystal structure of the L. pneumophila effector Lem10. The structure reveals a multidomain organization with the largest C-terminal domain showing strong structural similarity to the HD protein superfamily representatives. However, Lem10 lacks the catalytic His-Asp residue pair and does not show any in vitro phosphohydrolase enzymatic activity, typical for HD proteins. While the biological function of Lem10 remains elusive, our analysis shows that similar distinct features

SUBMITTER: Morar M 

PROVIDER: S-EPMC4715502 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature