4ELY

CCDBVFI:GYRA14EC

Replaces:  3KU8

Summary for 4ELY

• Entry DOI: 10.2210/pdb4ely/pdb
• Related: 3JRZ 3JSC 4elz
• Descriptor: DNA gyrase subunit A, CcdB, SULFATE ION, ... (5 entities in total)
• Functional Keywords: alpha+beta, topoisomerase, toxin-isomerase complex, toxin/isomerase
• Biological source: Shigella flexneri; More
• Cellular location: Cytoplasm (Potential): P0AES5
• Total number of polymer chains: 4
• Total formula weight: 59060.46

Authors

De Jonge, N.,Simic, R.,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

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: 22582791
DOI: 10.1111/j.1365-2958.2012.08069.x

Experimental method

X-RAY DIFFRACTION (1.932 Å)