Gyrase

From Proteopedia

spinqualitylabelsall models 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) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D Structure of Gyrase 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

Additional Resources

For additional information, see: Bacterial Infections

References

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