FunctionGyrase (Gyr) is a type of topoisomerase II in prokaryotes which unwinds double stranded DNA. The DNA Gyr cutting allows the formation of a negative DNA supercoil which enables replication of DNA[1] Gyr consists of 2 subunits: GyrA and GyrB. Reverse gyrase (Top-RG) is a type of topoisomerase I which catalyses the formation of positive DNA supercoil. [2] See also Isomerases.
RelevanceGyrA inhibitor Ciprofloxacin is used as antibiotic drug. Fluoroquinolones are Gyr inhibitors used in treatment of multi drug-resistant tuberculosis[3]
Structural highlights. A [4]. Water molecules shown as red spheres.
| |
3D Structure of Gyrase3D Structure of Gyrase
Updated on 04-April-2019
{"openlevels":0}
- Gyrase Subunit A
- 3l6v – GyrA C-terminal – Xanthomonas campestris
- 2y3p, 4ckl – EcGyrA N-terminal+simocylinone – Escherichia coli
- 1ajb - EcGyrA N-terminal+novobiocin
- 4ckk - EcGyrA N-terminal
- 1zi0, 1ab4 - EcGyrA C-terminal
- 1x75 – EcGyrA14+CcdB
- 4elz - GyrA fragment+CcdB – Vibrio fischeri
- 3ilw, 3ifz - MtGyrA ATPase domain – Mycobacterium tuberculosis
- 3uc1, 4g3n - MtGyrA C-terminal
- 1suu - GyrA C-terminal – Borrelia burgdorferi
- 3no0 - GyrA C-terminal – Aquifex aeolicus
- 3lpx – GyrA N-terminal – Colwellia psychrerithraea
- 4ely – GyrA residues 363-497 + CcdB – Shigella flexneri
- 4ddq – GyrA – Bacillus subtilis
- Gyrase Subunit B
- 3g75, 3g7b, 3g7e, 3ttz, 3u2d, 3u2k, 4p8o, 5cph, 5ctu, 5ctw, 5ctx, 5cty – GyrB ATP-binding domain residues 2-234 + inhibitor – Staphylococcus aureus
- 5d6p, 5d6q, 5d7c, 5d7d, 5d7r - SaGyrB ATP-binding domain + ligand
- 5npk, 5npp - SaGyrB residues 410-1491 + DNA
- 5mmn, 5mmo, 5mmp - EcGyrB ATP-binding domain + antibacterial
- 4urm, 4uro - SaGyrB N-terminal + antibiotic
- 2zjt, 3ig0, 3m4i - MtGyrB C-terminal
- 3cwv – GyrB truncated – Myxococcus xanthus
- 4wub, 4wuc, 4wud, 4xtj - EcGyrB N-terminal
- 1kzn, 1ei1, 1aj6 - EcGyrB N-terminal+ antibiotic
- 4duh, 4zvi, 5l3j - EcGyrB N-terminal+ inhibitor
- 4prv, 4prx, 4pu9 - EcGyrB N-terminal+ ADP
- 4hyp - EcGyrB residues 15-220 + inhibitor
- 1kij – GyrB ATPase domain+ antibiotic – Thermus thermophilus
- 4b6c - GyrB ATPase domain – Mycobacterium smegmatis
- 4gee, 4gfn, 4ggl, 4hxw, 4k4o, 4kfg, 4ksg, 4ksh, 4ktn – GyrB + inhibitor – Enterococcus faecalis
- 3zkb, 3zkd - MtGyrB ATPase domain + AMPPNP
- 3zm7 - MtGyrB ATPase domain + AMPPCP
- 4bae - MtGyrB ATPase domain (mutant) + inhibitor
- Gyrase Subunit A+Subunit B
- 2xco, 2xcq - SaGyrB C-terminal/SaGyrA N-terminal
- 4plb - SaGyrB C-terminal/SaGyrA N-terminal +DNA
- 2xcr, 2xcs, 4bul - SaGyrB C-terminal/SaGyrA N-terminal (mutant)+DNA
- 2xct - SaGyrB C-terminal/SaGyrA N-terminal (mutant) +DNA+ antibiotic
- 4tma - SaGyrB C-terminal- + SaGyrA N-terminal + Gyr inhibitor YACG
- 3nuh – EcGyrA+EcGyrB
- 5cdn, 5cdo, 5cdp, 6fqv – SaGyrA + SaGyrB + DNA
- 5cdq, 6fqm, 6fqs - SaGyrB + GyrA + DNA + antibiotic
- 5cdm – SaGyrA + SaGyrB (mutant) + DNA
- 5cdr – SaGyrA (mutant) + SaGyrB (mutant) + DNA
- 4z2c, 4z2d - SpGyrB + GyrA + DNA – Streptococcus pneumoniae
- 4z2e - SpGyrB + GyrA + DNA + antibiotic
- 5bs3, 5iwi, 5iwm - SaGyrB + GyrA + DNA + inhibitor
- 5bs8, 5bta, 5btd, 5btg, 5btl - MtGyrB + GyrA + DNA + antibiotic
- 5btc, 5btf, 5bti, 5btn - MtGyrB + GyrA (mutant) + DNA + antibiotic
- Reverse Gyrase
Additional ResourcesAdditional Resources
For additional information, see: Bacterial Infections
ReferencesReferences
- ↑ Reece RJ, Maxwell A. DNA gyrase: structure and function. Crit Rev Biochem Mol Biol. 1991;26(3-4):335-75. PMID:1657531 doi:http://dx.doi.org/10.3109/10409239109114072
- ↑ Napoli A, Valenti A, Salerno V, Nadal M, Garnier F, Rossi M, Ciaramella M. Functional interaction of reverse gyrase with single-strand binding protein of the archaeon Sulfolobus. Nucleic Acids Res. 2005 Jan 26;33(2):564-76. Print 2005. PMID:15673717 doi:http://dx.doi.org/10.1093/nar/gki202
- ↑ Aubry A, Pan XS, Fisher LM, Jarlier V, Cambau E. Mycobacterium tuberculosis DNA gyrase: interaction with quinolones and correlation with antimycobacterial drug activity. Antimicrob Agents Chemother. 2004 Apr;48(4):1281-8. PMID:15047530
- ↑ Singh SB, Kaelin DE, Wu J, Miesel L, Tan CM, Meinke PT, Olsen D, Lagrutta A, Bradley P, Lu J, Patel S, Rickert KW, Smith RF, Soisson S, Wei C, Fukuda H, Kishii R, Takei M, Fukuda Y. Oxabicyclooctane-linked novel bacterial topoisomerase inhibitors as broad spectrum antibacterial agents. ACS Med Chem Lett. 2014 Mar 12;5(5):609-14. doi: 10.1021/ml500069w. eCollection, 2014 May 8. PMID:24900889 doi:http://dx.doi.org/10.1021/ml500069w
