3jsc
CcdBVfi-FormI-pH7.0
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCcdB(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. Structural and thermodynamic characterization of Vibrio fischeri CcdB.,De Jonge N, Hohlweg W, Garcia-Pino A, Respondek M, Buts L, Haesaerts S, Lah J, Zangger K, Loris R J Biol Chem. 2010 Feb 19;285(8):5606-13. Epub 2009 Dec 2. PMID:19959472[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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