Gyrase: Difference between revisions

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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]] }}
<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==


'''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<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]].


==3D Structure of Gyrase==
==Relevance==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
GyrA inhibitor [[Ciprofloxacin]] is used as antibiotic drug.  Fluoroquinolones are Gyr inhibitors used in treatment of multi drug-resistant tuberculosis<ref>PMID:15047530</ref>
{{#tree:id=OrganizedByTopic|openlevels=0|


*Gyrase Subunit A
== 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.


**[[3l6v]] – GyrA C-terminal – ''Xanthomonas campestris'' <br />
==3D Structure of Gyrase==
**[[2wl2]], [[2y3p]], [[4ckl]] – EcGyrA N-terminal+simocylinone – ''Escherichia coli''<br />
[[Gyrase 3D Structures]]
**[[1ajb]] - EcGyrA N-terminal+novobiocin<br />
**[[4ckk]] - EcGyrA N-terminal<br />
**[[1zi0]], [[1ab4]] - EcGyrA C-terminal<br />
**[[3ku8]] – EcGyrA fragment+CcdB<br />
**[[1x75]] – EcGyrA14+CcdB<br />
**[[3kua]], [[4elz]] - GyrA fragment+CcdB – ''Vibrio fischeri''<br />
**[[3ilw]], [[3ifz]] - MtGyrA ATPase domain – ''Mycobacterium tuberculosis''<br />
**[[3uc1]], [[4g3n]] - MtGyrA C-terminal<br />
**[[1suu]] - GyrA C-terminal – ''Borrelia burgdorferi''<br />
**[[3no0]] - GyrA C-terminal – ''Aquifex aeolicus''<br />
**[[3lpx]] – GyrA N-terminal – ''Colwellia psychrerithraea''<br />
**[[4ely]] – GyrA residues 363-497 + CcdB – ''Shigella flexneri''<br />
**[[4ddq]] – GyrA – ''Bacillus subtilis''<br />
 
*Gyrase Subunit B
 
**[[3g75]], [[3g7b]], [[3g7e]] – GyrB+thiazole inhibitor – ''Staphylococcus aureus''<br />
**[[3ttz]], [[3u2d]], [[3u2k]] – SaGyrB + pyrrolamide inhibitor<br />
**[[2zjt]], [[3ig0]], [[3m4i]] - MtGyrB C-terminal<br />
**[[3cwv]] – GyrB truncated – ''Myxococcus xanthus''<br />
**[[1kzn]], [[1ei1]] - EcGyrB N-terminal+clorobiocin<br />
**[[1aj6]] - EcGyrB N-terminal+novobiocin<br />
**[[4duh]] - EcGyrB N-terminal+ inhibitor<br />
**[[4hyp]] - EcGyrB + inhibitor<br />
**[[1kij]] – GyrB domain+novobiocin – ''Thermus thermophilus''<br />
**[[4b6c]] - GyrB ATPase domain – ''Mycobacterium smegmatis''<br />
**[[4gee]], [[4gfn]], [[4ggl]], [[4hxw]], [[4k4o]], [[4kfg]], [[4ksg]], [[4ksh]], [[4ktn]] – GyrB + inhibitor – ''Enterococcus faecalis''<br />
**[[3zkb]], [[3zkd]] - MtGyrB ATPase domain + AMPPNP<br />
**[[3zm7]] - MtGyrB ATPase domain + AMPPCP<br />
**[[4bae]] - MtGyrB ATPase domain (mutant) + inhibitor<br />
 
*Gyrase Subunit A+Subunit B
 
**[[2xco]], [[2xcq]] - SaGyrB C-terminal-SaGyrA N-terminal fusion<br />
**[[2xcr]], [[2xcs]], [[4bul]] - SaGyrB C-terminal-SaGyrA N-terminal fusion (mutant)+DNA<br />
**[[2xct]] - SaGyrB C-terminal-SaGyrA N-terminal fusion (mutant) +DNA+ ciprofloxacin<br />
**[[3nuh]] – EcGyrA+EcGyrB


*Reverse Gyrase
</StructureSection>


**[[1gku]] – AfTop-RG – ''Archaeoglobus fulgidus''<br />
**[[1gl9]] - AfTop-RG+ADPNP<br />
**[[3oiy]], [[3p4y]] – TmTop-RG helicase domain – ''Thermotoga maritima''<br />
**[[4ddt]], [[4ddu]], [[4ddv]], [[4ddw]], [[4ddx]] - TmTop-RG
}}
==Additional Resources==
==Additional Resources==
For additional information, see: [[Bacterial Infections]]
For additional information, see: [[Bacterial Infections]]

Latest revision as of 13:21, 21 July 2019

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

. A [4]. Water molecules shown as red spheres.

3D Structure of Gyrase

Gyrase 3D Structures


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)

Drag the structure with the mouse to rotate

Additional ResourcesAdditional Resources

For additional information, see: Bacterial Infections

ReferencesReferences

  1. Reece RJ, Maxwell A. DNA gyrase: structure and function. Crit Rev Biochem Mol Biol. 1991;26(3-4):335-75. PMID:1657531 doi:http://dx.doi.org/10.3109/10409239109114072
  2. 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:http://dx.doi.org/10.1093/nar/gki202
  3. 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
  4. 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:http://dx.doi.org/10.1021/ml500069w

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