Publication
Title
The ParE2-PaaA2 toxin-antitoxin complex from Escherichia coli O157 forms a heterodocecamer in solution and in the crystal
Author
Abstract
Escherichia coli O157 paaR2-paaA2-parE2 constitutes a unique three-component toxinantitoxin (TA) module encoding 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 is likely to form a heterododecamer. Crystals of the ParE2PaaA2 complex diffract to 3.8 angstrom resolution and belong to space group P3121 or P3221, with unit-cell parameters a = b = 142.9, c = 87.5 angstrom. The asymmetric unit is consistent with a particle of around 125 kDa, which is compatible with the solution data. Therefore, the ParE2PaaA2 complex is the largest toxinantitoxin complex identified to date and its quaternary arrangement is likely to be of biological significance.
Language
English
Source (journal)
Acta Chrystallographica Section F. - -
Publication
2012
ISSN
2053-230X
Volume/pages
68 :6 (2012) , p. 724-729
ISI
000305073600028
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 04.10.2018
Last edited 29.11.2021