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

TitleCrystallization of Doc and the Phd-Doc toxin-antitoxin complex.
Publication TypeJournal Article
Year of Publication2008
AuthorsGarcia-Pino, A., M-H. Dao-Thi, E. Gazit, R. David Magnuson, L. Wyns, and R. Loris
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
IssuePt 11
Date Published2008 Nov 1
Type of Articleta
KeywordsAntitoxins, Crystallization, Molecular Sequence Data, Multiprotein Complexes, Toxins, Biological, Viral Proteins, X-Ray Diffraction

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.

Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID18997335
PubMed Central IDPMC2581698
Grant ListR15 GM067668 / GM / NIGMS NIH HHS / United States