Regulation of DNA supercoiling in Escherichia coli: genetic basis of a compensatory mutation in DNA gyrase.
Preliminary crystallographic analysis of the ATP-hydrolysing domain of the Escherichia coli DNA gyrase B protein.
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-392
Crystal structure of an N-terminal fragment of the DNA gyrase B protein.
The interaction between coumarin drugs and DNA gyrase.
Identifying the catalytic residue of the ATPase reaction of DNA gyrase.
Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid films.
A ribosomal protein module in EF-G and DNA gyrase.
The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-220 OF MUTANT HIS-135
The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study.
The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin.
Identifying Lys359 as a critical residue for the ATP-dependent reactions of Drosophila DNA topoisomerase II.
Conformational changes in DNA gyrase revealed by limited proteolysis.
Identification of a residue involved in transition-state stabilization in the ATPase reaction of DNA gyrase.
Isoleucine 10 is essential for DNA gyrase B function in Escherichia coli.
The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes.
Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center.
Temperature-sensitive suppressor mutations of the Escherichia coli DNA gyrase B protein.
GHKL, an emergent ATPase/kinase superfamily.
gyrB-225, a mutation of DNA gyrase that compensates for topoisomerase I deficiency: investigation of its low activity and quinolone hypersensitivity.
DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5'-methyl group of the noviose.
An open conformation of the Thermus thermophilus gyrase B ATP-binding domain.
Backbone 1H, 13C and 15N resonance assignment of the N-terminal 24 kDa fragment of the gyrase B subunit from E. coli.
The role of GyrB in the DNA cleavage-religation reaction of DNA gyrase: a proposed two metal-ion mechanism.
Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance.
This protein is B subunit of DNA-gyrase, which catalyzes ATP hydrolysis. The A subunit of this enzyme catalyzes DNA brekage and religation (see M00137). PDB structure, 1ei1, corresponds to the N-terminal half of the B subunit of DNA-gyrase. The other region, C-terminal half of the B subunit is responsible for the interaction with DNA and the A subunit, according to the literature [19]. According to the literature [13] & [18], the reaction proceeds as follows; (1) Glu42 (of 1ei1) acts as a general base, to activate a water molecule, which must be in-line for a nucleophilic attack on the gamma-phosphate of ATP. Lys337 may stabilize the activated water during this reaction. (2) Lys337 stabilizes the transition-state, along with mainchain amide of resdiues 115-119. Magnesium ion, possibly bound to Asn46, stabilizes the transition-state.