PMID:15159578

Citation	Dao-Thi, MH, Van Melderen, L, De Genst, E, Buts, L, Ranquin, A, Wyns, L and Loris, R (2004) Crystallization of CcdB in complex with a GyrA fragment. Acta Crystallogr. D Biol. Crystallogr. 60:1132-4
Abstract	Plasmid addiction systems consist of a plasmid-encoded toxin-antidote pair that serves to stabilize low-copy-number plasmids in bacterial populations. CcdB, the toxin from the ccd system on the Escherichia coli F plasmid, acts as a gyrase poison. A 14 kDa fragment of gyrase, GyrA14, was found to bind to the toxin CcdB with an affinity of 1.75 x 10(-8) M. Crystals of the (GyrA14)(2) dimer in its free state belong to space group P4(3)2(1)2, with unit-cell parameters a = 86.4, c = 89.4 angstroms, and diffract to 2.4 angstroms. Crystals of the (GyrA14)(2)-(CcdB)(2) complex belong to space group P2(1)2(1)2(1), with a = 52.1, b = 83.3, c = 110.9 angstroms, and diffract to 2.8 angstroms resolution.
Links	PubMed Online version:10.1107/S0907444904007814
Keywords	Bacterial Proteins/chemistry; Bacterial Toxins/chemistry; Cloning, Molecular; Crystallography, X-Ray; DNA Gyrase/chemistry; Dimerization; Electrophoresis, Polyacrylamide Gel; Escherichia coli/metabolism; F Factor/metabolism; Plasmids/metabolism; Protein Binding; Protein Structure, Tertiary; Surface Plasmon Resonance; X-Ray Diffraction
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