Expression, purification, crystallization, and X-ray diffraction studies on a PadR-like protein from Bacillus cereus

초록

Transcriptional regulators that belong to the PadR family play a critical role in the regulation of various biologicalprocesses, such as detoxification, catabolism, toxin production, and antibiotic resistance. The structural basis of effectorand DNA recognition by PadR has recently been provided through our previous structural study. However, it is unclearwhether the mechanism is universally used by other PadR family members. As a first step to reveal the transcriptionregulatory mechanism of Bacillus cereus PadR-like protein (bcPLP), we expressed the bcPLP protein in Escherichia colicells and purified it to homogeneity by chromatographic methods. bcPLP was crystallized in PEG 3350 solutions. A bcPLPcrystal diffracted X-ray to 1.95Å resolution. Our analysis of the X-ray diffraction data indicates that the crystal belongs tospace group P21212 and has two bcPLP chains in the asymmetric unit.

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