Literature summary extracted from
Carr, S.B.; Makris, G.; Phillips, S.E.; Thomas, C.D.
Crystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus (2006), Acta Crystallogr. Sect. F, 62, 1164-1167.
Application
EC Number |
Application |
Comment |
Organism |
---|
5.6.2.2 |
pharmacology |
Topo II are attractive targets for design of antitumor agents |
Staphylococcus aureus |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
5.6.2.2 |
Protein expression performed in Escherichia coli B834 DE3 (plysS) |
Staphylococcus aureus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
5.6.2.2 |
first report of crystallization and preliminary X-ray analysis of the DNA-cleavage domain of a topoisomerase IV from a gram positive organism. Sparse-matrix screening used, Crystals of both protein fragments (GrlA56 and GrlA59) display a plate-like morphology and initially grow in tightly packed clusters. Crystallization and X-ray analysis of two different constructs of the A subunit of topoisomerase IV from Staphylococcus aureus (GrlA) are described. With a view to gaining further insight into the mode of inhibition of quinolone antibiotics against this enzyme |
Staphylococcus aureus |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
5.6.2.2 |
56000 |
- |
generated protein GrlA56 |
Staphylococcus aureus |
5.6.2.2 |
59000 |
- |
generated protein GrlA59 |
Staphylococcus aureus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.6.2.2 |
Staphylococcus aureus |
Q6G9K4 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.6.2.2 |
- |
Staphylococcus aureus |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
5.6.2.2 |
heterotetramer |
Two constructs of 56 and 59 kDa spanning the DNA-cleavage domain of the A subunit of topoisomerase IV from Staphylococcus aureus. All bacterial type IIA topoisomerases are A2B2 heterotetramers containing three discrete subunit interfaces which open and close sequentially in response to ATP binding and hydrolysis in order to effect DNA transport |
Staphylococcus aureus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
5.6.2.2 |
DNA topoisomerase IV |
type IIA DNA topoisomerase |
Staphylococcus aureus |
5.6.2.2 |
topoIV |
- |
Staphylococcus aureus |