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From Proteopedia
(Difference between revisions)
(New page: ==Gyrase (maybe something like 'Structure')== 0 <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page ''...) |
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| - | ==Gyrase | + | ==DNA Gyrase== 0 |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
This is a default text for your page '''Sandbox reserved 1225'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Sandbox reserved 1225'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == Function == | + | == '''Function''' == DNA Gyrase is a protein located mainly in Prokaryotes, specifically bacteria. It falls under the Topoisomerase family and can be referred to as Topoisomerase II. It is responsible for negatively induced supercoiling. This method of supercoiling is used to reduce the strain caused by the twists in DNA. It aids in compaction, as well as separation of DNA. As one can see, it plays a significant role in prokaryotes. |
| - | == Disease ==asdfadfasdf | ||
| - | == | + | == '''Disease''' == Researches specifically study this protein for multiple reasons. It could possibly help with antibacterial chemotherapy. |
| - | == Structural highlights == | + | == '''Relevance''' == |
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| + | == '''Structural highlights''' == The structure of DNA Gyrase consists of mainly two subunits. This First known as A contains the tyrosine which is responsible for cleavage. The second subunit B is responsible to the binding of ATPase’s active site. Both subunits work together to produce the negative supercoiling produced in DNA strands. | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
| - | == References == | + | == References == Schoeffler, A. J., May, A. P., & Berger, J. M. (2010). A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Research, 38(21), 7830-7844. doi:10.1093/nar/gkq665 |
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| + | Rahimi, H., Najafi, A., Eslami, H., Negahdari, B., & Moghaddam, M. M. (2016). Identification of novel bacterial DNA gyrase inhibitors: An in silico study. Journal Of Research In Pharmaceutical Sciences, 11(3), 250-258. | ||
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| + | Travers, A., & Muskhelishvili, G. (2015). DNA structure and function. FEBS Journal, 282(12), 2279-2295. doi:10.1111/febs.13307 | ||
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<references/> | <references/> | ||
Revision as of 20:23, 8 March 2017
==DNA Gyrase== 0
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== References == Schoeffler, A. J., May, A. P., & Berger, J. M. (2010). A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Research, 38(21), 7830-7844. doi:10.1093/nar/gkq665
Rahimi, H., Najafi, A., Eslami, H., Negahdari, B., & Moghaddam, M. M. (2016). Identification of novel bacterial DNA gyrase inhibitors: An in silico study. Journal Of Research In Pharmaceutical Sciences, 11(3), 250-258.
Travers, A., & Muskhelishvili, G. (2015). DNA structure and function. FEBS Journal, 282(12), 2279-2295. doi:10.1111/febs.13307
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
