Gyrase
From Proteopedia
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==3D Structure of Gyrase== | ==3D Structure of Gyrase== | ||
| - | ''Update | + | ''Update February 2013'' |
===Gyrase Subunit A=== | ===Gyrase Subunit A=== | ||
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[[3ku8]] – EcGyrA fragment+CcdB<br /> | [[3ku8]] – EcGyrA fragment+CcdB<br /> | ||
[[1x75]] – EcGyrA14+CcdB<br /> | [[1x75]] – EcGyrA14+CcdB<br /> | ||
| - | [[3kua]] - GyrA fragment+CcdB – ''Vibrio fischeri''<br /> | + | [[3kua]], [[4elz]] - GyrA fragment+CcdB – ''Vibrio fischeri''<br /> |
[[3ilw]], [[3ifz]] - MtGyrA N-terminal – ''Mycobacterium tuberculosis''<br /> | [[3ilw]], [[3ifz]] - MtGyrA N-terminal – ''Mycobacterium tuberculosis''<br /> | ||
[[3uc1]] - MtGyrA C-terminal<br /> | [[3uc1]] - MtGyrA C-terminal<br /> | ||
[[1suu]] - GyrA C-terminal – ''Borrelia burgdorferi''<br /> | [[1suu]] - GyrA C-terminal – ''Borrelia burgdorferi''<br /> | ||
[[3no0]] - GyrA C-terminal – ''Aquifex aeolicus''<br /> | [[3no0]] - GyrA C-terminal – ''Aquifex aeolicus''<br /> | ||
| - | [[3lpx]] – GyrA N-terminal – ''Colwellia psychrerithraea'' | + | [[3lpx]] – GyrA N-terminal – ''Colwellia psychrerithraea''<br /> |
| + | [[4ely]] – GyrA residues 363-497 + CcdB – ''Shigella flexneri'' | ||
===Gyrase Subunit B=== | ===Gyrase Subunit B=== | ||
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[[1kzn]], [[1ei1]] - EcGyrB N-terminal+clorobiocin<br /> | [[1kzn]], [[1ei1]] - EcGyrB N-terminal+clorobiocin<br /> | ||
[[1aj6]] - EcGyrB N-terminal+novobiocin<br /> | [[1aj6]] - EcGyrB N-terminal+novobiocin<br /> | ||
| + | [[4duh]] - EcGyrB N-terminal+ inhibitor<br /> | ||
[[1kij]] – GyrB domain+novobiocin – ''Thermus thermophilus''<br /> | [[1kij]] – GyrB domain+novobiocin – ''Thermus thermophilus''<br /> | ||
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[[1gku]] – AfTop-RG – ''Archaeoglobus fulgidus''<br /> | [[1gku]] – AfTop-RG – ''Archaeoglobus fulgidus''<br /> | ||
[[1gl9]] - AfTop-RG+ADPNP<br /> | [[1gl9]] - AfTop-RG+ADPNP<br /> | ||
| - | [[3oiy]] – | + | [[3oiy]] – TmTop-RG helicase domain – ''Thermotoga maritima'' |
| + | [[4ddt]], [[4ddu]], [[4ddv]], [[4ddw]], [[4ddx]] - TmTop-RG | ||
==Additional Resources== | ==Additional Resources== | ||
Revision as of 12:57, 4 February 2013
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 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
- ↑ 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
