Title | Structural and thermodynamic characterization of Vibrio fischeri CcdB. |
Publication Type | Journal Article |
Year of Publication | 2010 |
Authors | De Jonge, N., W. Hohlweg, A. Garcia-Pino, M. Respondek, L. Buts, S. Haesaerts, J. Lah, K. Zangger, and R. Loris |
Journal | J Biol Chem |
Volume | 285 |
Issue | 8 |
Pagination | 5606-13 |
Date Published | 2010 Feb 19 |
Type of Article | ta |
ISSN | 1083-351X |
Keywords | Aliivibrio fischeri, Bacterial Toxins, Hydrophobic and Hydrophilic Interactions, Nuclear Magnetic Resonance, Biomolecular, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Secondary, Thermodynamics |
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. |
DOI | 10.1074/jbc.M109.068429 |
Alternate Journal | J. Biol. Chem. |
PubMed ID | 19959472 |
PubMed Central ID | PMC2820787 |
Grant List | W 901-B12 / / Austrian Science Fund FWF / Austria |
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