Gyrase
From Proteopedia
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| - | [[Image:3L6V.jpg|left|300px|thumb| Crystal Structure of ''Xanthomonas campestris'' Gyrase A C-terminal Domain, [[3l6v]]]] | ||
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{{STRUCTURE_3uc1| PDB=3uc1 | SIZE=400| SCENE= |right|CAPTION=Gyrase type IIA subunit A C-terminal domain with Ca+2 (green), acetate and glycerol, [[3uc1]] }} | {{STRUCTURE_3uc1| PDB=3uc1 | SIZE=400| SCENE= |right|CAPTION=Gyrase type IIA subunit A C-terminal domain with Ca+2 (green), acetate and glycerol, [[3uc1]] }} | ||
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'''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> | ||
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==3D Structure of Gyrase== | ==3D Structure of Gyrase== | ||
Revision as of 10:28, 18 August 2014
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]
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3D Structure of Gyrase
Updated on 18-August-2014
Gyrase Subunit A
3l6v – GyrA C-terminal – Xanthomonas campestris
2wl2, 2y3p, 4ckl – EcGyrA N-terminal+simocylinone – Escherichia coli
1ajb - EcGyrA N-terminal+novobiocin
4ckk - EcGyrA N-terminal
1zi0, 1ab4 - EcGyrA C-terminal
3ku8 – EcGyrA fragment+CcdB
1x75 – EcGyrA14+CcdB
3kua, 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 – 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
4hyp - EcGyrB + inhibitor
1kij – GyrB domain+novobiocin – 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 fusion
2xcr, 2xcs, 4bul - 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, 3p4y – 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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