Product Details

Purity

>85% (SDS-PAGE)

Target Names

gyrA

Uniprot No.

P0AES4

Alternative Names

gyrA; hisW; nalA; parD; b2231; JW2225; DNA gyrase subunit A; EC 5.6.2.2

Species

Escherichia coli (strain K12)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

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.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein 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

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

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

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
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
Data indicate the existence of interactions between the fluoroquinolone C-7 ring and both GyrA and GyrB. PMID: 24497635
This new structure is entirely consistent with the mutations in GyrA that confer Simocyclinone D8 resistance. PMID: 24594357
The C-terminal part of McbA is crucial for DNA gyrase inhibition and antibiotic uptake. PMID: 24563033
binds to plasmid-encoded quinolone resistance protein Qnr PMID: 15616284
The low-resolution structure of the full-length A subunit (GyrA)was reported. PMID: 15698572
Analysis of DNA supercoiling by the E. coli GyrA C-terminal domain PMID: 15897198
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

Cytoplasm.

Protein Families

Type II topoisomerase GyrA/ParC subunit family

Database Links

KEGG: ecj:JW2225

STRING: 316385.ECDH10B_2390

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Recombinant Escherichia coli DNA gyrase subunit A (gyrA), partial

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