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

par Hadži, San;Garcia-Pino, Abel ;Martínez-Rodríguez, Sergio;Verschueren, Koen;Christensen-Dalsgaard, Mikkel;Gerdes, Kenn;Lah, Jurij;Loris, Remy
Référence Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 69, Pt 9, page (1052-1059)
Publication Publié, 2013-09

Article révisé par les pairs

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Résumé :

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 P2(1)2(1)2, with unit-cell parameters a = 129.0, b = 119.8, c = 33.4 Å, and diffracted to 3.0 Å 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 P3(2)21, with unit-cell parameters a = 134.5, c = 55.4 Å. These crystals diffracted to 2.2 Å 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 Å, β = 106.7°, and diffracted to 1.8 Å resolution.