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

  • Garcia-Pino A
  • Dao-Thi M
  • Gazit E
 et al. 
  • 15

    Readers

    Mendeley users who have this article in their library.
  • 6

    Citations

    Citations of this article.

Abstract

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.

Author-supplied keywords

  • Plasmid addiction
  • TA modules
  • Toxin-antitoxin

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text

Authors

  • Abel Garcia-Pino

  • Minh Hoa Dao-Thi

  • Ehud Gazit

  • Roy David Magnuson

  • Lode Wyns

  • Remy Loris

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free