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The ParE2-PaaA2 toxin-antitoxin complex from E. coli O157 forms a hetero-docecamer in solution and in the crystal
Tijdschriftbijdrage - Tijdschriftartikel
The Escherichia coli O157 paaR2-paaA2-parE2 constitutes a unique three-component toxin-antitoxin (TA) module with a toxin (ParE2) related to the classic parDE family, but with an unrelated antitoxin called PaaA2. The complex between PaaA2 and ParE2 was purified and characterized by analytical gel filtration, dynamic light scattering, and small-angle X-ray scattering. It consists of a particle with a radius of gyration of 3.95 nm and likely forms a hetero-dodecamer. Crystals of the PaaA2-ParE2 complex diffract to 3.8Å resolution and belong to space group P3121 or P3221 with unit cell a = b = 142.9Å, c = 87.5Å. The asymmetric unit is consistent with a particle of around 125 kDa, compatible with the solution data. Therefore, the PaaA2-ParE2 complex is the largest toxin-antitoxin complex identified so far and its quaternary arrangement is likely to be of biological significance.
Tijdschrift: Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
ISSN: 1744-3091
Volume: 68
Pagina's: 724-729
Jaar van publicatie:2012
Trefwoorden:structural biology, complementary methods in structural biology, bacterial toxin, bacterial stress response, toxin-antitoxin module, biophysics