Structural and Thermodynamic Characterization of Vibrio fischeri CcdB

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. Thi...

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Bibliographic Details
Published in:The Journal of biological chemistry 2010-02, Vol.285 (8), p.5606-5613
Main Authors: De Jonge, Natalie, Hohlweg, Walter, Garcia-Pino, Abel, Respondek, Michal, Buts, Lieven, Haesaerts, Sarah, Lah, Jurij, Zangger, Klaus, Loris, Remy
Format: Article
Language:English
Subjects:
Aliivibrio fischeri - chemistry
Bacterial Toxins - chemistry
Bacterial Toxins - genetics
Biophysics
Gyrase Poison
Hydrophobic and Hydrophilic Interactions
Nuclear Magnetic Resonance, Biomolecular
Protein Multimerization
Protein Structure and Folding
Protein Structure, Quaternary
Protein Structure, Secondary
Protein/Conformation
Protein/Stability
Protein/Structure
Thermodynamics
Toxin-Antitoxin
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M109.068429