Purified E. coli DNA Gyrase A protein (over expressed from E. coli)
Conjugate
Unconjugated
Target
Alternative Names
DNA gyrase subunit A; GyrA; HisW; NalA; ParD
Product Background
Antigen Description
DNA Gyrase A belongs to the topoisomerase gyrA/parC subunit family. 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. It is made up of two chains. The A chain is responsible for DNA breakage and rejoining; the B chain catalyzes ATP hydrolysis. The enzyme forms an A2B2 tetramer. When the enzyme transiently cleaves DNA a phosphotyrosine bond is formed between the gyrA and DNA.
Citations
Publication ()
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Background
DNA gyrase, a specialized type II topoisomerase that reshapes bacterial chromosomes by introducing a negative superhelix, plays an important role in compressing the genome and solving topological puzzles related to replication and transcription. The enzyme forms dynamic complexes with DNA larger than 100 bp, which must form and break protein-DNA interactions and rearrange sharply curved DNA pathways during each ATP-driven conformational cycle.
DNA gyrase is a kind of Isomeric tetramer, which consists of 2 GyrA and 2 GyrB subunits, and is arranged into a triple domain structure with double symmetry. The B subunit of DNA gyrase contains ATP binding site and hydrolysis site, while subunit A is responsible for DNA binding and entrapment. GyrA contains active-site tyrosine residues which are located in the helix-turn-helix motif of a catabolite activator protein (CAP)-like domain. GyrB contains a Topoisomerase-Primase (TOPRIM) domain, which seems to play a key role in the catalytic process, providing a binding site for divalent cations involved in DNA cleavage and reconnection. When phosphodiester bond is broken, the 5' end of the DNA is covalently attached to the enzyme via a tyrosine in the active site, producing a cleaved complex. The globular C-terminal domain (CTD) of DNA gyrase is different from other type II topoisomerases. It is the key to the unique introduction ability of DNA gyrase.
Figure 1. Composition of DNA gyrase (Source: Basu A, et al. 2016)
DNA gyrase in bacteria is also the target of clinical development of new antimicrobials and one of the main targets of broad-spectrum antimicrobials quinolones. Quinolones act by stabilizing the gyrase-DNA cleavage complex, the stabilization of which hinders replication forks and slows bacterial growth. Water-metal ion bridge in DNA gyrase A subunit mediates the binding of quinolones to DNA gyrase, while the common mutations of DNA gyrase in drug-resistant strains occur on some residues that form the water-metal ion bridge between enzyme and drug. In fact, the region between amino acids 67 and 106 in GyrA is called quinolone resistance determination region (QRDR). Creative Diagnostics offers monoclonal antibodies against DNA gyrase A, expressed by E. coli, for use in WB assays.
Alternative Names
DNA gyrase subunit A monoclonal antibody GyrA monoclonal antibody
References
1. Basu A, et al. Structural Dynamics and Mechanochemical Coupling in DNA Gyrase. J Mol Biol. 2016 May 8;428(9 Pt B):1833-45.
2. Spencer AC, et al. DNA Gyrase as a Target for Quinolones. Biomedicines. 2023 Jan 27;11(2):371.
3. Sutormin DA, et al. Diversity and Functions of Type II Topoisomerases. Acta Naturae. 2021 Jan-Mar;13(1):59-75.
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References
Evybactin is a DNA gyrase inhibitor that selectively kills Mycobacterium tuberculosis
Nat Chem Biol
Authors: Imai Y, Hauk G, Quigley J, Liang L, Son S, Ghiglieri M, Gates MF, Morrissette M, Shahsavari N, Niles S, Baldisseri D, Honrao C, Ma X, Guo JJ, Berger JM, Lewis K.
The antimicrobial resistance crisis requires the introduction of novel antibiotics. The use of conventional broad-spectrum compounds selects for resistance in off-target pathogens and harms the microbiome. This is especially true for Mycobacterium tuberculosis, where treatment requires a 6-month course of antibiotics. Here we show that a novel antimicrobial from Photorhabdus noenieputensis, which we named evybactin, is a potent and selective antibiotic acting against M. tuberculosis. Evybactin targets DNA gyrase and binds to a site overlapping with synthetic thiophene poisons. Given the conserved nature of DNA gyrase, the observed selectivity against M. tuberculosis is puzzling. We found that evybactin is smuggled into the cell by a promiscuous transporter of hydrophilic compounds, BacA. Evybactin is the first, but likely not the only, antimicrobial compound found to employ this unusual mechanism of selectivity.
A novel gyrase inhibitor from toxin-antitoxin system expressed by Staphylococcus aureus
FEBS J
Authors: Kato F, Yamaguchi Y, Inouye K, Matsuo K, Ishida Y, Inouye M.
Toxin-antitoxin (TA) systems consist of a toxin inhibiting essential cellular functions (such as DNA, RNA and protein synthesis), and its cognate antitoxin neutralizing the toxicity. Recently, we identified a TA system termed TsbA/TsbT in the Staphylococcus aureus genome. The induction of the tsbT gene in Escherichia coli halted both DNA and RNA synthesis, reduced supercoiled plasmid and resulted in increasingly relaxed DNA. These results suggested that DNA gyrase was the target of TsbT. In addition, TsbT inhibited both E. coli and S. aureus DNA gyrase activity and induced linearization of plasmid DNA in vitro. Taken together, these results demonstrate that the TsbT toxin targets DNA gyrase in vivo. Site-directed mutagenesis experiments showed that the E27 and D37 residues in TsbT are critical for toxicity. Secondary structure prediction combining the analysis of vacuum-ultraviolet circular-dichroism spectroscopy and neural network method demonstrated that the 22nd-32nd residues of TsbT form an α-helix structure, and that the E27 residue is located around the centre of the α-helix segment. These findings give new insights not only into S. aureus TA systems, but also into bacterial toxins targeting DNA topoisomerases.
COA
Publication 
Figure 1. Composition of DNA gyrase
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