Structural characterization of a conserved, calcium-dependent periplasmic protease from Legionella pneumophila.

ABSTRACT: The bacterial dinucleotide second messenger c-di-GMP has emerged as a central molecule in regulating bacterial behavior, including motility and biofilm formation. Proteins for the synthesis and degradation of c-di-GMP and effectors for its signal transmission are widely used in the bacterial domain. Previous work established the GGDEF-EAL domain-containing receptor LapD as a central switch in Pseudomonas fluorescens cell adhesion. LapD senses c-di-GMP inside the cytosol and relays this signal to the outside by the differential recruitment of the periplasmic protease LapG. Here we identify the core components of an orthologous system in Legionella pneumophila. Despite only moderate sequence conservation at the protein level, key features concerning the regulation of LapG are retained. The o

SUBMITTER: Chatterjee D 

PROVIDER: S-EPMC3416269 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature