Gyrase

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Revision as of 07:10, 23 December 2010

Image:3L6V.jpg
Crystal Structure of Xanthomonas campestris Gyrase A C-terminal Domain, 3l6v

Crystal Structure of the Xanthomonas campestris Gyrase A C-terminal Domain, 3l6v

Drag the structure with the mouse to rotate

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]

Contents

3D Structure of Gyrase

Gyrase Subunit A

3l6v – GyrA C-terminal – Xanthomonas campestris
2wl2 – EcGyrA N-terminal+simocylinone – Escherichia coli
1ajb - EcGyrA N-terminal+novobiocin
1zi0, 1ab4 - EcGyrA C-terminal
3ku8 – EcGyrA fragment+CcdB
1x75 – EcGyrA14+CcdB
3kua - GyrA fragment+CcdB – Vibrio fischeri
3ilw, 3ifz - MtGyrA N-terminal – Mycobacterium tuberculosis
1suu - GyrA C-terminal – Borrelia burgdorferi
3no0 - GyrA C-terminal – Aquifex aeolicus

Gyrase Subunit B

3g75, 3g7b, 3g7e – GyrB+thiazole inhibitor – Staphylococcus aureus
2zjt, 3ig0, 3m4i - MtGyrB C-terminal
3cwv – GyrB truncated – Myxococcus xanthus
1kzn, 1ei1 - EcGyrB N-terminal+clorobiocin
1aj6 - EcGyrB N-terminal+novobiocin
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 – Top-RG helicase domain – Thermotoga maritima

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

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Michal Harel, Alexander Berchansky, David Canner, Joel L. Sussman

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