Gyrase
From Proteopedia
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{{STRUCTURE_3uc1| PDB=3uc1 | SIZE=350| SCENE= |right|CAPTION=Gyrase type IIA subunit A C-terminal domain with Ca+2 (green), acetate and glycerol, [[3uc1]] }} | {{STRUCTURE_3uc1| PDB=3uc1 | SIZE=350| SCENE= |right|CAPTION=Gyrase type IIA subunit A C-terminal domain with Ca+2 (green), acetate and glycerol, [[3uc1]] }} | ||
| + | ==Function== | ||
'''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> See also [[Isomerases]]. | '''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> See also [[Isomerases]]. | ||
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| + | ==Relevance== | ||
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| + | GyrA inhibitor [[Ciprofloxacin]] is used as antibiotic drug. | ||
==3D Structure of Gyrase== | ==3D Structure of Gyrase== | ||
Revision as of 11:14, 29 February 2016
Contents |
Function
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] See also Isomerases.
Relevance
GyrA inhibitor Ciprofloxacin is used as antibiotic drug.
3D Structure of Gyrase
Updated on 29-February-2016
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
