Structural highlights
Function
VFR_PSEAE Can bind cyclic AMP. Is a global regulator of virulence factor expression and is required for exotoxin A and protease production.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
Crystal Structure of Pseudomonas aeruginosa Virulence Factor Regulator.,Cordes TJ, Worzalla GA, Ginster AM, Forest KT J Bacteriol. 2011 Jun 10. PMID:21665969[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cordes TJ, Worzalla GA, Ginster AM, Forest KT. Crystal Structure of Pseudomonas aeruginosa Virulence Factor Regulator. J Bacteriol. 2011 Jun 10. PMID:21665969 doi:10.1128/JB.00666-10
