title: 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.
authors.affiliation: University of Wisconsin-Madison, Department of Bacteriology, 1550 Linden Dr., Madison, WI 53706, USA.
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Cordes
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Worzalla
authors.forename: Aaron M
authors.initials: AM
authors.lastname: Ginster
authors.forename: Katrina T
authors.initials: KT
authors.lastname: Forest
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D003460:Crystallization; D002373:Cyclic AMP Receptor Protein / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D037521:Virulence Factors / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D002373:Cyclic AMP Receptor Protein; C091090:Vfr protein, Pseudomonas aeruginosa; D037521:Virulence Factors