Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae.

The genome of Vibrio cholerae encodes two higBA toxin-antitoxin (TA) modules that are activated by amino-acid starvation. Here, the TA complex of the second module, higBA2, as well as the C-terminal domain of the
corresponding HigA2 antitoxin, have been purified and crystallized. The HigBA2 complex crystallized in two crystal forms. Crystals of form I belonged to space group P21212, with unit-cell parameters a = 129.0, b = 119.8, c = 33.4 A ? , and diffracted to 3.0 A ? resolution. The asymmetric unit is likely to contain a single complex consisting of two toxin monomers and one antitoxin dimer. The second crystal form crystallized in space group P3221, with unit-cell parameters a = 134.5, c = 55.4 A ? . These crystals diffracted to 2.2 A ? resolution and probably contain a complex with a different stoichiometry. Crystals of the C-terminal domain of HigA2 belonged to space group C2, with unit-cell parameters a = 115.4, b = 61.2, c = 73.8 A ? , = 106.7, and diffracted to 1.8 A ? resolution.

Jaar van publicatie:2013

Trefwoorden:Toxin-antitoxin module, Structural biology, Macromolecular Crystallography, Persister