Structural and thermodynamic characterization of Vibrio fischeri CcdB

Natalie De Jonge, Walter Hohlweg, Abel Garcia Pino, Michal Respondek, Lieven Buts, Sarah Haesaerts, Jurij Lah, Klaus Zangger, Remy Loris

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

CcdBVfi from Vibrio fischeri is a member of the CcdB family of toxins that poison covalent gyrase-DNA complexes. In solution CcdBVfi is a dimer that unfolds to the corresponding monomeric components in a two-state fashion. In the unfolded state, the monomer retains a partial secondary structure. This observation correlates well with the crystal and NMR structures of the protein, which show a dimer with a hydrophobic core crossing the dimer interface. In contrast to its F plasmid homologue, CcdBVfi possesses a rigid dimer interface, and the apparent relative rotations of the two subunits are due to structural plasticity of the monomer. CcdBVfi shows a number of non-conservative substitutions compared with the F plasmid protein in both the CcdA and the gyrase binding sites. Although variation in the CcdA interaction site likely determines toxin-antitoxin specificity, substitutions in the gyrase-interacting region may have more profound functional implications.
Original languageEnglish
Pages (from-to)5606-5613
Number of pages8
JournalJ. Biol. Chem.
Volume285
Publication statusPublished - 2010

Keywords

  • Toxin-antitoxin modules
  • structural biology
  • Stress regulation in bacteria
  • protein stability

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