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

TitleCrystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae.
Publication TypeJournal Article
Year of Publication2013
AuthorsHadži, S., A. Garcia-Pino, S. Martinez-Rodriguez, K. Verschueren, M. Christensen-Dalsgaard, K. Gerdes, J. Lah, and R. Loris
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume69
IssuePt 9
Pagination1052-9
Date Published2013 Sep
Type of Articleta
ISSN1744-3091
Abstract

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.

DOI10.1107/S1744309113021490
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID23989162
PubMed Central IDPMC3758162