Structural and Thermodynamic Characterization of Vibrio fischeri CcdB

• DOI: 10.1074/jbc.m109.068429
• Publication Date: 2009-12-04T01:18:24Z
• Authors: Natalie De Jonge; Walter Hohlweg; Abel Garcia-Pino; Michal Respondek; Lieven Buts; Sarah Haesaerts; Jurij Lah; Klaus Zangger; Remy Loris
• Keywords: Characterization

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