Summary for 4ELZ
| Entry DOI | 10.2210/pdb4elz/pdb |
| Related | 3JRZ 3JSC |
| Descriptor | DNA gyrase subunit A, CcdB, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | alpha+beta, topoisomerase, toxin-isomerase complex, toxin/isomerase |
| Biological source | Vibrio fischeri More |
| Cellular location | Cytoplasm (By similarity): Q5E5J7 |
| Total number of polymer chains | 4 |
| Total formula weight | 58374.92 |
| Authors | De Jonge, N.,Simic, M.,Buts, L.,Haesaerts, S.,Roelants, K.,Garcia-Pino, A.,Sterckx, Y.,De Greve, H.,Lah, J.,Loris, R. (deposition date: 2012-04-11, release date: 2012-05-30, Last modification date: 2023-09-13) |
| Primary citation | De Jonge, N.,Simic, M.,Buts, L.,Haesaerts, S.,Roelants, K.,Garcia-Pino, A.,Sterckx, Y.,De Greve, H.,Lah, J.,Loris, R. Alternative interactions define gyrase specificity in the CcdB family. Mol.Microbiol., 84:965-978, 2012 Cited by PubMed Abstract: Toxin-antitoxin (TA) modules are small operons associated with stress response of bacteria. F-plasmid CcdB(F) was the first TA toxin for which its target, gyrase, was identified. Plasmidic and chromosomal CcdBs belong to distinct families. Conserved residues crucial for gyrase poisoning activity of plasmidic CcdBs are not conserved among these families. Here we show that the chromosomal CcdB(Vfi) from Vibrio fischeri is an active gyrase poison that interacts with its target via an alternative energetic mechanism. Changes in the GyrA14-binding surface of the Vibrio and F-plasmid CcdB family members illustrate neutral drift where alternative interactions can be used to achieve the same functionality. Differences in affinity between V. fischeri and F-plasmid CcdB for gyrase and their corresponding CcdA antitoxin possibly reflect distinct roles for TA modules located on plasmids and chromosomes. PubMed: 22582791DOI: 10.1111/j.1365-2958.2012.08069.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
