The ParE2-PaaA2 toxin-antitoxin complex from E. coli O157 forms a hetero-docecamer in solution and in the crystal

Yann Sterckx, Abel Garcia Pino, Sarah Haesaerts, Thomas Jove, Lieselotte Geerts, Viktor Sakellaris, Laurence Van Melderen, Remy Loris

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)724-729
Number of pages6
JournalActa Crystallogr F Struct Biol Commun
Volume68
Publication statusPublished - 2012

Keywords

  • structural biology
  • complementary methods in structural biology
  • bacterial toxin
  • bacterial stress response
  • toxin-antitoxin module
  • biophysics

Fingerprint

Dive into the research topics of 'The ParE2-PaaA2 toxin-antitoxin complex from E. coli O157 forms a hetero-docecamer in solution and in the crystal'. Together they form a unique fingerprint.

Cite this