DNA negative supercoiling activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / DNA-templated DNA replication / chromosome / response to antibiotic / DNA binding / ATP binding ...DNA negative supercoiling activity / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / DNA-templated DNA replication / chromosome / response to antibiotic / DNA binding / ATP binding / metal ion binding / cytoplasm Similarity search - Function
Topoisomerase II; domain 5 / Topoisomerase II, domain 5 / Topoisomerase, domain 3 / Topoisomerase; domain 3 / Rossmann fold - #670 / Gyrase A; domain 2 - #40 / DNA gyrase, subunit A / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller ...Topoisomerase II; domain 5 / Topoisomerase II, domain 5 / Topoisomerase, domain 3 / Topoisomerase; domain 3 / Rossmann fold - #670 / Gyrase A; domain 2 - #40 / DNA gyrase, subunit A / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller / Topoisomerase (Topo) IIA-type catalytic domain profile. / DNA gyrase subunit B, TOPRIM domain / DNA gyrase, subunit B / DNA topoisomerase, type IIA, subunit B / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA gyrase B subunit, C-terminal / DNA gyrase B subunit, carboxyl terminus / DNA topoisomerase, type IIA, subunit B, domain 2 / DNA gyrase B / DNA topoisomerase, type IIA / DNA topoisomerase, type IIA, conserved site / DNA topoisomerase II signature. / TopoisomeraseII / DNA topoisomerase, type IIA, subunit B, C-terminal / Toprim domain / DNA topoisomerase, type IIA-like domain superfamily / Toprim domain profile. / TOPRIM domain / Gyrase A; domain 2 / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Alpha-Beta Complex / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta Similarity search - Domain/homology
B: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A D: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A E: 5'-D(*5UA*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' F: 5'-D(*5UA*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' S: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A U: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A V: 5'-D(*AP*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' W: 5'-D(*AP*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' hetero molecules
B: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A D: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A E: 5'-D(*5UA*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' F: 5'-D(*5UA*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' hetero molecules
S: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A U: DNA GYRASE SUBUNIT B, DNA GYRASE SUBUNIT A V: 5'-D(*AP*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' W: 5'-D(*AP*GP*CP*CP*GP*TP*AP*GP*GP*GP*CP*CP*CP*TP*AP*CP*GP *GP*CP*TP)-3' hetero molecules
Mass: 461.579 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C25H27N5O2S / Comment: antibiotic*YM
Compound details
ENGINEERED RESIDUE IN CHAIN B, TYR 123 TO PHE ENGINEERED RESIDUE IN CHAIN D, TYR 123 TO PHE ...ENGINEERED RESIDUE IN CHAIN B, TYR 123 TO PHE ENGINEERED RESIDUE IN CHAIN D, TYR 123 TO PHE ENGINEERED RESIDUE IN CHAIN S, TYR 123 TO PHE ENGINEERED RESIDUE IN CHAIN U, TYR 123 TO PHE
Nonpolymer details
ACETYLATED ADENOSINE : IN HIGHER RESOLUTION 2.1A STRUCTURE WAS EXTRA DENSITY ON ONE END OF DNA, ...ACETYLATED ADENOSINE : IN HIGHER RESOLUTION 2.1A STRUCTURE WAS EXTRA DENSITY ON ONE END OF DNA, MODELLED AS ACETYLATED ADENOSINE.
Sequence details
THIS IS A FUSION TRUNCATE IN WHICH THE C-TERMINAL RESIDUE OF GYRB (F644) IS FUSED TO THE N-TERMINAL ...THIS IS A FUSION TRUNCATE IN WHICH THE C-TERMINAL RESIDUE OF GYRB (F644) IS FUSED TO THE N-TERMINAL RESIDUE OF GYRA (A2). CATALYTIC TYROSINE (123) HAS BEEN MUTATED TO PHENYLALANINE
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 4.06 Å3/Da / Density % sol: 69 % / Description: NONE