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| [[Image:3L6V.jpg|left|350px]] | | <StructureSection load='' size='350' side='right' caption='Gyrase subunit A N-terminal (cyan) and subunit B C-terminal (magenta) complex with DNA, inhibitor, sulfate and Mn+2 ion (purple) (PDB entry [[4plb]])' scene='41/410321/Cv/1'> |
| | ==Function== |
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| <applet load='3l6v.pdb' size='350' frame='true' align='right' scene="Gyrase/Gyrase_starting_scene/1" caption= 'Crystal Structure of the Xanthomonas campestris Gyrase A C-terminal Domain, [[3l6v]]' />
| | '''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<ref>PMID:1657531</ref> 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:15673717</ref> See also [[Isomerases]]. |
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| '''3D Structure of Gyrase''' <br />
| | ==Relevance== |
| The image at the left is a Crystal Structure of the Gyrase A C-terminal Domain([[3l6v]])
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| ==Gyrase==
| | GyrA inhibitor [[Ciprofloxacin]] is used as antibiotic drug. Fluoroquinolones are Gyr inhibitors used in treatment of multi drug-resistant tuberculosis<ref>PMID:15047530</ref> |
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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.<br /><br /><br /> | | == Structural highlights == |
| | <scene name='41/410321/Cv/5'>Gyrase subunit A N-terminal and subunit B C-terminal complex with DNA and inhibitor</scene>. A <scene name='41/410321/Cv/6'>potential drug interacts with both DNA strands and in the hydrophobic pocket between subunits A and B</scene><ref>PMID:24900889</ref>. Water molecules shown as red spheres. |
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| ==3D Structure of Gyrase== | | ==3D Structure of Gyrase== |
| | [[Gyrase 3D Structures]] |
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| ===Gyrase Subunit A===
| | </StructureSection> |
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| [[3l6v]] – GyrA C-terminal – Xanthomonas campestris <br />
| | ==Additional Resources== |
| [[2wl2]] – EcGyrA N-terminal+simocylinone – Escherichia coli<br />
| | For additional information, see: [[Bacterial Infections]] |
| [[1ajb]] - EcGyrA N-terminal+novobiocin<br />
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| [[1zi0]], [[1ab4]] - EcGyrA C-terminal<br />
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| [[1x75]] – EcGyrA14+CcdB<br />
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| [[3ilw]] - MtGyrA N-terminal – Mycobacterium tuberculosis<br />
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| [[1suu]] - GyrA C-terminal – Borrelia burgdorferi<br />
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| ===Gyrase Subunit B=== | | ==References== |
| | <References /> |
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| [[3g75]], [[3g7b]], [[3g7e]] – GyrB+thiazole inhibitor – Staphylococcus aureus<br /> | | [[Category:Topic Page]] |
| [[2cjt]] - MtGyrB C-terminal<br />
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| [[3cwv]] – GyrB truncated – Myxococcus xanthus<br />
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| [[1kzn]], [[1ei1]] - EcGyrB N-terminal+clorobiocin<br />
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| [[1kij]] – GyrB domain+novobiocin – Thermus thermophilus<br />
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| ===Reverse Gyrase===
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| [[1gku]] – AfTop-RG – Archaeoglobus fulgidus<br />
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| [[1gl9]] - AfTop-RG+ADPNP<br />
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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[1] 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. [2] See also Isomerases.
Relevance
GyrA inhibitor Ciprofloxacin is used as antibiotic drug. Fluoroquinolones are Gyr inhibitors used in treatment of multi drug-resistant tuberculosis[3]
Structural highlights
Gyrase subunit A N-terminal and subunit B C-terminal complex with DNA and inhibitor. A potential drug interacts with both DNA strands and in the hydrophobic pocket between subunits A and B[4]. Water molecules shown as red spheres.
3D Structure of Gyrase
Gyrase 3D Structures
- ↑ Reece RJ, Maxwell A. DNA gyrase: structure and function. Crit Rev Biochem Mol Biol. 1991;26(3-4):335-75. PMID:1657531 doi:https://dx.doi.org/10.3109/10409239109114072
- ↑ Napoli A, Valenti A, Salerno V, Nadal M, Garnier F, Rossi M, Ciaramella M. Functional interaction of reverse gyrase with single-strand binding protein of the archaeon Sulfolobus. Nucleic Acids Res. 2005 Jan 26;33(2):564-76. Print 2005. PMID:15673717 doi:https://dx.doi.org/10.1093/nar/gki202
- ↑ Aubry A, Pan XS, Fisher LM, Jarlier V, Cambau E. Mycobacterium tuberculosis DNA gyrase: interaction with quinolones and correlation with antimycobacterial drug activity. Antimicrob Agents Chemother. 2004 Apr;48(4):1281-8. PMID:15047530
- ↑ Singh SB, Kaelin DE, Wu J, Miesel L, Tan CM, Meinke PT, Olsen D, Lagrutta A, Bradley P, Lu J, Patel S, Rickert KW, Smith RF, Soisson S, Wei C, Fukuda H, Kishii R, Takei M, Fukuda Y. Oxabicyclooctane-linked novel bacterial topoisomerase inhibitors as broad spectrum antibacterial agents. ACS Med Chem Lett. 2014 Mar 12;5(5):609-14. doi: 10.1021/ml500069w. eCollection, 2014 May 8. PMID:24900889 doi:https://dx.doi.org/10.1021/ml500069w
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Additional Resources
For additional information, see: Isomerases
References
