Journal
JOURNAL OF BACTERIOLOGY
Volume 193, Issue 16, Pages 4069-4074Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00666-10
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Funding
- U.S. Department of Agriculture Hatch
- National Institutes of Health (NIH) [GM59721]
- UW-Madison NIH
- Beckman Scholar's Award
- Merck
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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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