2KMT
NMR solution structure of Vibrio fischeri CcdB
Summary for 2KMT
| Entry DOI | 10.2210/pdb2kmt/pdb |
| NMR Information | BMRB: 16135 |
| Descriptor | CcdB (1 entity in total) |
| Functional Keywords | toxin |
| Biological source | Vibrio fischeri |
| Total number of polymer chains | 2 |
| Total formula weight | 23759.44 |
| Authors | Zangger, K. (deposition date: 2009-08-04, release date: 2009-12-01, Last modification date: 2024-05-15) |
| Primary citation | De Jonge, N.,Hohlweg, W.,Garcia-Pino, A.,Respondek, M.,Buts, L.,Haesaerts, S.,Lah, J.,Zangger, K.,Loris, R. Structural and Thermodynamic Characterization of Vibrio fischeri CcdB. J.Biol.Chem., 285:5606-5613, 2010 Cited by PubMed 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. PubMed: 19959472DOI: 10.1074/jbc.M109.068429 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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