Recombinant Escherichia coli DNA gyrase subunit A (gyrA) (S83W)

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Code CSB-EP365190ENV(A4M1)
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 85% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
gyrA; hisW; nalA; parD; b2231; JW2225; DNA gyrase subunit A; EC
Escherichia coli (strain K12)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
101.0 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Tris-based buffer,50% glycerol
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase IV (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than many other bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical. The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box.; Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Gene References into Functions
  1. analysis of gyrase mutations in E.coli that could be responsible for increased quinolone resistive mechanisms among enteric pathogens; docking studies revealed displacement of quinolone binding site in mutated protein complex which resulted in lower binding energy as compared to the normal one PMID: 29300775
  2. The present study was undertaken to better understand the dynamic behavior of the gyrA in Enterotoxigenic Escherichia coli [ETEC] and to decipher the structural changes associated with mutations, Ser83Leu and Ser83Leu/Asp87Asn, leading to ciprofloxacin antibiotic resistance in ETEC gyrA. PMID: 27753544
  3. Data indicate the existence of interactions between the fluoroquinolone C-7 ring and both GyrA and GyrB. PMID: 24497635
  4. This new structure is entirely consistent with the mutations in GyrA that confer Simocyclinone D8 resistance. PMID: 24594357
  5. The C-terminal part of McbA is crucial for DNA gyrase inhibition and antibiotic uptake. PMID: 24563033
  6. binds to plasmid-encoded quinolone resistance protein Qnr PMID: 15616284
  7. The low-resolution structure of the full-length A subunit (GyrA)was reported. PMID: 15698572
  8. Analysis of DNA supercoiling by the E. coli GyrA C-terminal domain PMID: 15897198
  9. acquisition of a fourth resistance mutation significantly increased fitness especially with the addition of a parC mutation (Topoisomerase IV) to a low-fitness strain carrying resistance mutations in gyrA (DNA Gyrase) and marR (drug efflux regulation) PMID: 19662169

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Subcellular Location
Protein Families
Type II topoisomerase GyrA/ParC subunit family
Database Links
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