Structural evidence suggests that antiactivator ExsD from Pseudomonas aeruginosa is a DNA binding protein.

ABSTRACT: The opportunistic pathogen P. aeruginosa utilizes a type III secretion system (T3SS) to support acute infections in predisposed individuals. In this bacterium, expression of all T3SS-related genes is dependent on the AraC-type transcriptional activator ExsA. Before host contact, the T3SS is inactive and ExsA is repressed by the antiactivator protein ExsD. The repression, thought to occur through direct interactions between the two proteins, is relieved upon opening of the type III secretion (T3S) channel when secretion chaperone ExsC sequesters ExsD. We have solved the crystal structure of Delta20ExsD, a protease-resistant fragment of ExsD that lacks only the 20 amino terminal residues of the wild-type protein at 2.6 A. Surprisingly the structure revealed similarities between ExsD and the

SUBMITTER: Bernhards RC 

PROVIDER: S-EPMC2760357 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature