Crystallization of Doc and the Phd-Doc toxin-antitoxin complex.
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.
Garcia-Pino
Abel
A
Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussel, Belgium. agarciap@vub.ac.be
Dao-Thi
Minh-Hoa
MH
Gazit
Ehud
E
Magnuson
Roy David
RD
Wyns
Lode
L
Loris
Remy
R
D000992:Antitoxins / Q000737:chemistry*; D003460:Crystallization; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry*; D014118:Toxins, Biological / Q000737:chemistry*; D014764:Viral Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
D000992:Antitoxins; C083664:Doc protein, Enterobacteria phage P1; D046912:Multiprotein Complexes; C083665:Phd protein, Enterobacteria phage P1; D014118:Toxins, Biological; D014764:Viral Proteins