2OZ6

Crystal Structure of Virulence Factor Regulator from Pseudomonas aeruginosa in complex with cAMP

Summary for 2OZ6

• Entry DOI: 10.2210/pdb2oz6/pdb
• Descriptor: Virulence Factor Regulator, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: winged helix, helix-turn-helix, transcription factor, camp-binding proteins, camp receptor protein, nucleotide binding proteins, dna-binding proteins, dna binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 24200.66

Authors

Cordes, T.J.,Bright, A.R.,Forest, K.T. (deposition date: 2007-02-24, release date: 2008-03-04, Last modification date: 2023-08-30)

Primary citation

Cordes, T.J.,Worzalla, G.A.,Ginster, A.M.,Forest, K.T.
Crystal Structure of the Pseudomonas aeruginosa Virulence Factor Regulator.
J.Bacteriol., 193:4069-4074, 2011

PubMed 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.

PubMed: 21665969
DOI: 10.1128/JB.00666-10

Experimental method

X-RAY DIFFRACTION (2.8 Å)