Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of Cif, a Virulence Factor Secreted by Pseudomonas Aeruginosa

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Acta Crystallographica. Section F - Structural Biology and Crystallization Communications


Geisel School of Medicine


The opportunistic pathogen Pseudomonas aeruginosa secretes a protein that triggers the accelerated degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) in airway epithelial cells. This protein, which is known as the CFTR inhibitory factor (Cif), acts as a virulence factor and may facilitate airway colonization by P. aeruginosa. Based on sequence similarity Cif appears to be an epoxide hydrolase (EH), but it lacks several of the conserved features found in the active sites of canonical members of the EH family. Here, the crystallization of purified recombinant Cif by vapor diffusion is reported. The crystals formed in space group C2, with unit-cell parameters a = 167.4, b = 83.6, c = 88.3 Å, = 100.6°. The crystals diffracted to 2.39 Å resolution on a rotating-anode source. Based on the calculated Matthews coefficient (2.2 Å3 Da-1), it appears that the asymmetric unit contains four molecules.



Original Citation

Bahl CD, MacEachran DP, O'Toole GA, Madden DR. Purification, crystallization and preliminary X-ray diffraction analysis of Cif, a virulence factor secreted by Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):26-8. doi: 10.1107/S1744309109047599. Epub 2009 Dec 25. PMID: 20057063; PMCID: PMC2805529.