Aarhus University Seal / Aarhus Universitets segl

Andreas Bøggild

The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

The bacterial relBE locus encodes a toxin-antitoxin complex in which the toxin, RelE, is capable of cleaving mRNA in the ribosomal A site cotranslationally. The antitoxin, RelB, both binds and inhibits RelE, and regulates transcription through operator binding and conditional cooperativity controlled by RelE. Here, we present the crystal structure of the intact Escherichia coli RelB(2)E(2) complex at 2.8 Å resolution, comprising both the RelB-inhibited RelE and the RelB dimerization domain that binds DNA. RelE and RelB associate into a V-shaped heterotetrameric complex with the ribbon-helix-helix (RHH) dimerization domain at the apex. Our structure supports a model in which relO is optimally bound by two adjacent RelB(2)E heterotrimeric units, and is not compatible with concomitant binding of two RelB(2)E(2) heterotetramers. The results thus provide a firm basis for understanding the model of conditional cooperativity at the molecular level.
Original languageEnglish
JournalStructure
Volume20
Issue10
Pages (from-to)1641–1648
Number of pages8
ISSN0969-2126
DOIs
Publication statusPublished - 10 Oct 2012

See relations at Aarhus University Citationformats

ID: 48840835