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Crystallization of Doc and the Phd-Doc toxin-antitoxin complex.

par Garcia-Pino, Abel ;Dao-Thi, Minh-Hoa;Gazit, Ehud;Magnuson, Roy David;Wyns, Lode;Loris, Remy
Référence Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 64, Pt 11, page (1034-1038)
Publication Publié, 2008-11

Article révisé par les pairs

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Résumé :

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 A, beta = 93.0 degrees . These crystals diffracted to 2.5 A 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 A, beta = 99.3 degrees , and diffracted to 1.9 A 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 A and diffracted to 2.4 A resolution using synchrotron radiation.