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The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity
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 controlle...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507626/ https://www.ncbi.nlm.nih.gov/pubmed/22981948 http://dx.doi.org/10.1016/j.str.2012.08.017 |
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author | Bøggild, Andreas Sofos, Nicholas Andersen, Kasper R. Feddersen, Ane Easter, Ashley D. Passmore, Lori A. Brodersen, Ditlev E. |
author_facet | Bøggild, Andreas Sofos, Nicholas Andersen, Kasper R. Feddersen, Ane Easter, Ashley D. Passmore, Lori A. Brodersen, Ditlev E. |
author_sort | Bøggild, Andreas |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3507626 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Cell Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-35076262012-12-14 The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity Bøggild, Andreas Sofos, Nicholas Andersen, Kasper R. Feddersen, Ane Easter, Ashley D. Passmore, Lori A. Brodersen, Ditlev E. Structure Short Article 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. Cell Press 2012-10-10 /pmc/articles/PMC3507626/ /pubmed/22981948 http://dx.doi.org/10.1016/j.str.2012.08.017 Text en © 2012 ELL & Excerpta Medica. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license |
spellingShingle | Short Article Bøggild, Andreas Sofos, Nicholas Andersen, Kasper R. Feddersen, Ane Easter, Ashley D. Passmore, Lori A. Brodersen, Ditlev E. The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity |
title | The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity |
title_full | The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity |
title_fullStr | The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity |
title_full_unstemmed | The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity |
title_short | The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity |
title_sort | crystal structure of the intact e. coli relbe toxin-antitoxin complex provides the structural basis for conditional cooperativity |
topic | Short Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507626/ https://www.ncbi.nlm.nih.gov/pubmed/22981948 http://dx.doi.org/10.1016/j.str.2012.08.017 |
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