Structural highlights
4ely is a 4 chain structure with sequence from "achromobacter_fischeri"_(beijerinck_1889)_bergey_et_al._1930 "achromobacter fischeri" (beijerinck 1889) bergey et al. 1930 and "shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927. This structure supersedes the now removed PDB entry 3ku8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Ligands: | , |
Related: | 3jsc, 3jrz, 4elz |
Gene: | gyrA, GYRASE, S2444, SF2311 ("Shigella paradysenteriae" Weldin 1927), ccdB ("Achromobacter fischeri" (Beijerinck 1889) Bergey et al. 1930) |
Activity: | DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[GYRA_SHIFL] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (By similarity).
Publication Abstract from PubMed
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.
Alternative interactions define gyrase specificity in the CcdB family.,De Jonge N, Simic M, Buts L, Haesaerts S, Roelants K, Garcia-Pino A, Sterckx Y, De Greve H, Lah J, Loris R Mol Microbiol. 2012 Jun;84(5):965-978. doi: 10.1111/j.1365-2958.2012.08069.x., Epub 2012 May 14. PMID:22582791[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2012 Jun;84(5):965-978. doi: 10.1111/j.1365-2958.2012.08069.x., Epub 2012 May 14. PMID:22582791 doi:10.1111/j.1365-2958.2012.08069.x