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Updated: Jun 1, 2026

A Fluorescence-based Method to Study Bacterial Gene Regulation in Infected Tissues
Published on: February 19, 2019
Crystal structure of the Pseudomonas aeruginosa virulence factor regulator
Timothy J Cordes1, Gregory A Worzalla, Aaron M Ginster
1University of Wisconsin-Madison, Department of Bacteriology, 1550 Linden Dr., Madison, WI 53706, USA.
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.
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