Crystal structure of the Pseudomonas aeruginosa virulence factor regulator.

ABSTRACT: Virulence factor regulator (Vfr) enhances Pseudomonas aeruginosa pathogenicity through its role as a global transcriptional regulator. The crystal structure of Vfr shows that it is a winged-helix DNA-binding protein like its homologue cyclic AMP receptor protein (CRP). In addition to an expected primary cyclic AMP-binding site, a second ligand-binding site is nestled between the N-terminal domain and the C-terminal helix-turn-helix domain. Unlike CRP, Vfr is a symmetric dimer in the absence of DNA. Removal of seven disordered N-terminal residues of Vfr prevents the growth of P. aeruginosa.

SUBMITTER: Cordes TJ 

PROVIDER: S-EPMC3147669 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature