4FXI

Crystal structure of the isolated E. coli RelE toxin, P21 form

Replaces:  3KHA

Summary for 4FXI

• Entry DOI: 10.2210/pdb4fxi/pdb
• Related: 2KC8 2KC9 3KHA
• Descriptor: mRNA interferase RelE, SULFATE ION (3 entities in total)
• Functional Keywords: toxin/antitoxin system, toxin, nuclease, translational control, stress response, relb, ribosome, b-me on cys50
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 34285.13

Authors

Brodersen, D.E.,Boggild, A.,Sofos, N. (deposition date: 2012-07-03, release date: 2012-08-29, Last modification date: 2024-10-09)

Primary citation

Boggild, A.,Sofos, N.,Andersen, K.R.,Feddersen, A.,Easter, A.D.,Passmore, L.A.,Brodersen, D.E.
The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity.
Structure, 20:1641-1648, 2012

PubMed Abstract: 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 RelB2E2 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 RelB2E heterotrimeric units, and is not compatible with concomitant binding of two RelB2E2 heterotetramers. The results thus provide a firm basis for understanding the model of conditional cooperativity at the molecular level.

PubMed: 22981948
DOI: 10.1016/j.str.2012.08.017

Experimental method

X-RAY DIFFRACTION (1.8003 Å)