Crystallization of Doc and the Phd-Doc toxin-antitoxin complex
Crystallization of Doc and the Phd-Doc toxin-antitoxin complex
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DOI：
10.1107/s1744309108031722
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发表时间：
2008-11-01
影响因子：
0.9
通讯作者：
Loris, Remy
中科院分区：
文献类型：
--
作者：
Garcia-Pino, Abel;Dao-Thi, Minh-Hoa;Loris, Remy
phd/doc成瘾系统负责溶原性噬菌体P1在大肠杆菌中以其质粒形式的稳定遗传，并且是细菌毒素-抗毒素模块家族的原型。Doc的His 66 Tyr突变体（Doc（H66 Y））以空间群P2（1）结晶，晶胞参数a = 53.1，B = 198.0，c = 54.1埃，β = 93.0度。这些晶体衍射至2.5埃分辨率，并且在不对称单元中可能包含Doc的四个二聚体。Doc（H66 Y）与Phd（Phd（52- 73 Se））的22-氨基酸C-末端肽的复合物以空间群C2结晶，晶胞参数a = 111.1，B = 38.6，c = 63.3埃，β = 99.3度，并衍射至1.9埃分辨率。完整的野生型Phd-Doc复合物的晶体属于空间群P3（1）21或P3（2）21，具有尺寸为a = B = 48.9，c = 354.9埃的细长晶胞，并且使用同步辐射衍射至2.4埃分辨率。
The phd/doc addiction system is responsible for the stable inheritance of lysogenic bacteriophage P1 in its plasmidic form in Escherichia coli and is the archetype of a family of bacterial toxin-antitoxin modules. The His66Tyr mutant of Doc (Doc(H66Y)) was crystallized in space group P2(1), with unit-cell parameters a = 53.1, b = 198.0, c = 54.1 angstrom, beta = 93.0 degrees. These crystals diffracted to 2.5 angstrom resolution and probably contained four dimers of Doc in the asymmetric unit. Doc(H66Y) in complex with a 22-amino-acid C-terminal peptide of Phd (Phd(52-73Se)) was crystallized in space group C2, with unit-cell parameters a = 111.1, b = 38.6, c = 63.3 angstrom, beta = 99.3 degrees, and diffracted to 1.9 angstrom resolution. Crystals of the complete wild-type Phd-Doc complex belonged to space group P3(1)21 or P3(2)21, had an elongated unit cell with dimensions a = b = 48.9, c = 354.9 angstrom and diffracted to 2.4 angstrom resolution using synchrotron radiation.