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Structural and thermodynamic characterization of Vibrio fischeri CcdB.


ABSTRACT: CcdB(Vfi) from Vibrio fischeri is a member of the CcdB family of toxins that poison covalent gyrase-DNA complexes. In solution CcdB(Vfi) 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, CcdB(Vfi) possesses a rigid dimer interface, and the apparent relative rotations of the two subunits are due to structural plasticity of the monomer. CcdB(Vfi) 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.

SUBMITTER: De Jonge N 

PROVIDER: S-EPMC2820787 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature

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Structural and thermodynamic characterization of Vibrio fischeri CcdB.

De Jonge Natalie N   Hohlweg Walter W   Garcia-Pino Abel A   Respondek Michal M   Buts Lieven L   Haesaerts Sarah S   Lah Jurij J   Zangger Klaus K   Loris Remy R  

The Journal of biological chemistry 20091202 8


CcdB(Vfi) from Vibrio fischeri is a member of the CcdB family of toxins that poison covalent gyrase-DNA complexes. In solution CcdB(Vfi) 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, C  ...[more]

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