Gyrase

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[[Image:3L6V.jpg|left|300px|thumb| Crystal Structure of ''Xanthomonas campestris'' Gyrase A C-terminal Domain, [[3l6v]]]]
[[Image:3L6V.jpg|left|300px|thumb| Crystal Structure of ''Xanthomonas campestris'' Gyrase A C-terminal Domain, [[3l6v]]]]
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<applet load='1suu.pdb' size='400' frame='true' align='right' scene= caption= 'Crystal Structure of the Xanthomonas campestris Gyrase A C-terminal Domain, [[1suu]]' />
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<applet load='3uc1.pdb' size='400' frame='true' align='right' scene= caption= 'Crystal Structure of the Xanthomonas campestris Gyrase A C-terminal Domain, [[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. <ref>PMID:16397501</ref>
'''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. <ref>PMID:16397501</ref>

Revision as of 09:49, 4 November 2012

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, 3uc1

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

Update June 2012

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 - 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

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
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

Proteopedia Page Contributors and Editors (what is this?)

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

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