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Crystallization and preliminary crystal structure analysis of the ligand‐binding domain of PqsR (MvfR), the

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The opportunistic bacterial pathogen Pseudomonas aeruginosa employs three transcriptional regulators, LasR, RhlR and PqsR, to control the transcription of a large subset of its genes in a cell‐density‐dependent process known as quorum sensing. Here, the recombinant production, crystallization and structure solution of the ligand‐binding domain of PqsR (MvfR), the LysR‐type transcription factor that responds to the Pseudomonas quinolone signal (PQS), a quinolone‐based quorum‐sensing signal that is unique to P. aeruginosa and possibly a small number of other bacteria, is reported. PqsR regulates the expression of many virulence genes and may therefore be an interesting drug target. The ligand‐binding domain (residues 91–319) was produced as a fusion with SUMO, and hexagonal‐shaped crystals of purified PqsR_91–319 were obtained using the vapour‐diffusion method. Crystallization in the presence of a PQS precursor allowed data collection to 3.25 Å resolution on a synchrotron beamline, and initial phases have been obtained using single‐wavelength anomalous diffraction data from seleno‐l‐methionine‐labelled crystals, revealing the space group to be P6522, with unit‐cell parameters a = b = 116–120, c = 115–117 Å.
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Document Type: Research Article

Publication date: September 1, 2012

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