Title | Crystallization of CcdB in complex with a GyrA fragment. |
Publication Type | Journal Article |
Year of Publication | 2004 |
Authors | Dao-Thi, M-H., L. Van Melderen, E. De Genst, L. Buts, A. Ranquin, L. Wyns, and R. Loris |
Journal | Acta Crystallogr D Biol Crystallogr |
Volume | 60 |
Issue | Pt 6 |
Pagination | 1132-4 |
Date Published | 2004 Jun |
ISSN | 0907-4449 |
Keywords | Bacterial Proteins, Bacterial Toxins, Cloning, Molecular, Crystallography, X-Ray, Dimerization, DNA Gyrase, Electrophoresis, Polyacrylamide Gel, Escherichia coli, F Factor, Plasmids, Protein Binding, Protein Structure, Tertiary, Surface Plasmon Resonance, X-Ray Diffraction |
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. |
DOI | 10.1107/S0907444904007814 |
Alternate Journal | Acta Crystallogr. D Biol. Crystallogr. |
PubMed ID | 15159578 |
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