Ontology highlight
ABSTRACT:
SUBMITTER: De Jonge N
PROVIDER: S-EPMC2820787 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
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]