Crystallization of CcdB in complex with a GyrA fragment

被引:18
作者
Dao-Thi, MH
Van Melderen, L
De Genst, E
Buts, L
Ranquin, A
Wyns, L
Loris, R
机构
[1] Free Univ Brussels VIB, Lab Ultrastruct, B-1050 Brussels, Belgium
[2] Free Univ Brussels, Inst Biol & Med, Lab Genet Procaryotes, Gosselies, Belgium
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷
关键词
D O I
10.1107/S0907444904007814
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 1.75x10(-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 Angstrom, and diffract to 2.4 Angstrom. 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 Angstrom, and diffract to 2.8 Angstrom resolution.
引用
收藏
页码:1132 / 1134
页数:3
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