Gyrase

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Template:STRUCTURE 3uc1

Gyrase (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. 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. ^[1]

3D Structure of Gyrase

Update February 2013

Gyrase Subunit A

3l6v – GyrA C-terminal – Xanthomonas campestris
2wl2, 2y3p – EcGyrA N-terminal+simocylinone – Escherichia coli
1ajb - EcGyrA N-terminal+novobiocin
1zi0, 1ab4 - EcGyrA C-terminal
3ku8 – EcGyrA fragment+CcdB
1x75 – EcGyrA14+CcdB
3kua, 4elz - GyrA fragment+CcdB – Vibrio fischeri
3ilw, 3ifz - MtGyrA N-terminal – Mycobacterium tuberculosis
3uc1 - 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

Gyrase Subunit B

3g75, 3g7b, 3g7e – GyrB+thiazole inhibitor – Staphylococcus aureus
3ttz, 3u2d, 3u2k – SaGyrB + pyrrolamide inhibitor
2zjt, 3ig0, 3m4i - MtGyrB C-terminal
3cwv – GyrB truncated – Myxococcus xanthus
1kzn, 1ei1 - EcGyrB N-terminal+clorobiocin
1aj6 - EcGyrB N-terminal+novobiocin
4duh - EcGyrB N-terminal+ inhibitor
1kij – GyrB domain+novobiocin – Thermus thermophilus

Gyrase Subunit A+Subunit B

2xco, 2xcq - SaGyrB C-terminal-SaGyrA N-terminal fusion
2xcr, 2xcs - SaGyrB C-terminal-SaGyrA N-terminal fusion (mutant)+DNA
2xct - SaGyrB C-terminal-SaGyrA N-terminal fusion (mutant) +DNA+ ciprofloxacin
3nuh – EcGyrA+EcGyrB

Reverse Gyrase

1gku – AfTop-RG – Archaeoglobus fulgidus
1gl9 - AfTop-RG+ADPNP
3oiy – TmTop-RG helicase domain – Thermotoga maritima 4ddt, 4ddu, 4ddv, 4ddw, 4ddx - TmTop-RG

Additional Resources

For additional information, see: Bacterial Infections

References

1. ↑ Gore J, Bryant Z, Stone MD, Nollmann M, Cozzarelli NR, Bustamante C. Mechanochemical analysis of DNA gyrase using rotor bead tracking. Nature. 2006 Jan 5;439(7072):100-4. PMID:16397501 doi:10.1038/nature04319