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Publication Abstract from PubMed
Virulence Factor Regulator (Vfr) enhances Pseudomonas aeruginosa pathogenicity through its role as a global transcriptional regulator. The crystal structure of Vfr shows it is a winged-helix DNA-binding protein like its homologue cAMP Receptor Protein (CRP). In addition to an expected primary cAMP-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 growth of P. aeruginosa.
